What is Protein Kinase C (PKC)?

Protein Kinase C (PKC) is a family of protein kinase enzymes crucial in cell biology. These enzymes function by phosphorylating hydroxyl groups on serine and threonine amino acid residues of other proteins, thereby regulating their activity. PKC plays a significant role in various signal transduction cascades within the cell.

What is the official classification and identifier for Protein Kinase C?

Protein Kinase C is classified under the Enzyme Commission (EC) number 2.7.11.13 and has the CAS registry number 141436-78-4.

What cellular signals typically activate Protein Kinase C enzymes?

PKC enzymes are generally activated by intracellular signals such as an increase in the concentration of diacylglycerol (DAG) or calcium ions (Ca2+).

How many distinct isozymes of Protein Kinase C exist in humans?

In humans, there are fifteen known isozymes belonging to the Protein Kinase C family.

What are the three main subfamilies of PKC, and how are they categorized?

The PKC family is divided into three subfamilies based on their requirements for specific second messengers: conventional (or classical) PKCs, novel PKCs, and atypical PKCs.

What are the activation requirements for conventional (c)PKC isoforms?

Conventional PKC isoforms, including alpha, beta I, beta II, and gamma, require the presence of diacylglycerol (DAG), calcium ions (Ca2+), and a phospholipid such as phosphatidylserine for activation.

What specific molecules are required for the activation of novel (n)PKC isoforms?

Novel PKC isoforms, such as delta, epsilon, eta, and theta, require diacylglycerol (DAG) for activation but do not require calcium ions (Ca2+).

What distinguishes the activation mechanism of atypical (a)PKC isoforms?

Atypical PKC isoforms, including protein kinase M zeta and iota/lambda, are unique in that they require neither calcium ions (Ca2+) nor diacylglycerol (DAG) for activation.

What is the evolutionary origin of the Protein Kinase C family?

The PKC family is ancient, with evidence suggesting its presence in fungi and its existence in the last common ancestor of opisthokonts. In jawed vertebrates, the family expanded from five ancestral members through genome duplication events.

Describe the basic structure of all Protein Kinase C enzymes.

All PKC enzymes are composed of two primary domains: a regulatory domain and a catalytic domain, which houses the active site. These two domains are linked together by a flexible hinge region.

How conserved is the catalytic domain of PKC compared to other protein kinases?

The catalytic region of PKC is highly conserved among the various PKC isoforms. It also shows significant, though lesser, similarity to the catalytic regions of other serine/threonine-specific protein kinases.

What determines the different requirements for second messengers among PKC isoforms?

The differences in second messenger requirements (like Ca2+ or DAG) among PKC isoforms are primarily determined by variations within their regulatory domains. While the regulatory regions are similar within each subfamily (conventional, novel, atypical), they differ significantly between the subfamilies.

Which specific PKC isoforms have had their crystal structures elucidated?

The crystal structures of the catalytic regions have been determined for two specific PKC isoforms: PKC theta and PKC iota.

What is the function of the C1 domain within the regulatory region of PKC?

The C1 domain serves as a binding site for diacylglycerol (DAG), a key second messenger. It can also bind to non-physiological analogues like phorbol esters, which are often used experimentally.

Are the C1 domains of all PKC isoforms capable of binding DAG?

No, while the C1 domain is present in all isoforms, it is functional and capable of binding DAG only in conventional and novel PKC isoforms. The C1 domain in atypical PKCs cannot bind DAG or phorbol esters.

What is the role of the C2 domain in PKC?

The C2 domain functions as a sensor for calcium ions (Ca2+). This function is particularly important in the activation of conventional PKC isoforms.

What is the pseudosubstrate region of PKC, and what is its function?

The pseudosubstrate region is a short amino acid sequence within the PKC molecule that mimics a substrate protein. It binds to the catalytic domain's active site, keeping the enzyme in an inactive state until specific activation signals cause its release.

How do calcium ions and diacylglycerol lead to PKC activation?

When calcium ions (Ca2+) and diacylglycerol (DAG) concentrations increase, they bind to the C2 and C1 domains of PKC, respectively. This binding recruits the enzyme to the cell membrane, facilitates the release of the pseudosubstrate from the catalytic site, and thereby activates the enzyme.

What crucial step must occur before PKC can become catalytically active?

Before PKC can become catalytically active, it must undergo proper folding into the correct conformation. This conformational state is dependent on the phosphorylation of its catalytic region.

What is the approximate amino acid sequence similarity between the catalytic regions of PKC and PKB/Akt?

The catalytic regions of PKB (also known as Akt) and PKC share approximately 40% amino acid sequence similarity.

What are the three key phosphorylation sites found in conventional and novel PKC isoforms?

Conventional and novel PKC isoforms possess three critical phosphorylation sites: the activation loop, the turn motif, and the hydrophobic motif.

How do atypical PKC isoforms differ in their phosphorylation patterns compared to conventional and novel isoforms?

Atypical PKC isoforms are phosphorylated only on the activation loop and the turn motif, whereas conventional and novel isoforms are phosphorylated on these sites as well as the hydrophobic motif.

Which upstream kinase is primarily responsible for initiating the phosphorylation of PKC?

3-phosphoinositide-dependent protein kinase-1 (PDPK1) is the upstream kinase that initiates the phosphorylation process for PKC activation, starting with the activation loop.

What is the consensus sequence of PKC enzymes similar to, and why?

The consensus sequence of PKC enzymes is similar to that of Protein Kinase A (PKA) because both contain basic amino acids located near the serine or threonine residue targeted for phosphorylation.

Can you provide examples of proteins that are phosphorylated by PKC?

Yes, PKC enzymes phosphorylate various substrates, including MARCKS proteins, MAP kinase, transcription factor inhibitor IκB, the vitamin D3 receptor (VDR), Raf kinase, calpain, and the epidermal growth factor receptor.

What is the process of 'substrate presentation' in PKC activation?

Substrate presentation is an activation mechanism where activated PKC enzymes translocate to the plasma membrane, thereby gaining access to their substrate proteins.

What effect does microgravity have on PKC activation, and what is a known consequence?

Microgravity has been observed to disrupt the translocation of PKC to the cell membrane. This disruption is linked to the immunodeficiency experienced by astronauts.

What are some of the diverse functions attributed to PKC in cellular processes?

PKC is involved in a wide range of functions, including receptor desensitization, modulation of membrane structure, regulation of gene transcription, mediation of immune responses, control of cell growth, and roles in learning and memory.

Why are PKC isoforms sometimes referred to as 'memory kinases'?

PKC isoforms are sometimes called 'memory kinases' due to their involvement in processes related to learning and memory, and deficits in PKC signaling have been noted as an early abnormality in Alzheimer's disease.

How does PKC contribute to the immune system's function?

PKC plays a role in the immune system by phosphorylating CARD-CC family proteins, which subsequently leads to the activation of NF-κB, a key transcription factor involved in immune responses.

How does the cell-type specificity of PKC effects arise?

The effects of PKC are cell-type specific because the particular substrate proteins available for phosphorylation vary depending on the cell type, reflecting differences in protein expression.

What is the potential role of PKC in cancer progression?

PKC activation, particularly by tumor promoters like phorbol esters, may contribute to cancer progression by phosphorylating transcription activators, potentially leading to increased expression of oncogenes.

What is the general implication of PKC mutations and protein levels in cancer?

The prevalence of loss-of-function mutations and reduced PKC protein levels in cancer suggests that Protein Kinase C generally acts as a tumor suppressor.

How are PKC enzymes implicated in vascular diseases?

PKC enzymes are implicated in vascular diseases by mediating vascular permeability. They are linked to conditions associated with hyperglycemia in diabetes mellitus and to endothelial injury caused by cigarette smoke.

What is ruboxistaurin, and what condition might it help treat?

Ruboxistaurin is a Protein Kinase C inhibitor that shows potential benefit in the treatment of peripheral diabetic nephropathy.

Can you name some naturally occurring selective inhibitors of PKC?

Chelerythrine, miyabenol C, myricitrin, and gossypol are mentioned as naturally occurring selective PKC inhibitors.

What is Darovasertib, and what is its current research application?

Darovasertib is an investigational new drug that is currently undergoing efficacy trials for the treatment of metastatic uveal melanoma.

What is ingenol mebutate, and what is its approved medical use?

Ingenol mebutate, derived from the plant *Euphorbia peplus*, is an FDA-approved PKC activator used for treating actinic keratosis.

What is 12-O-Tetradecanoylphorbol-13-acetate (PMA or TPA), and how does it interact with PKC?

PMA or TPA is a compound that mimics diacylglycerol (DAG) and can activate the classical isoforms of PKC. It is often used in combination with ionomycin.

What is the role of ionomycin when used with PMA or TPA?

Ionomycin provides the necessary calcium-dependent signals that, when combined with PMA or TPA, help activate certain PKC isoforms.

Who is credited with the discovery of Protein Kinase C?

Yasutomi Nishizuka is credited with the discovery of protein kinase C.

What are the different classes of PKC found in jawed vertebrates, and how did they evolve?

The PKC classes in jawed vertebrates originated from five ancestral PKC family members. Their diversification and expansion into different classes occurred through genome duplication events.

What is the function of the catalytic region of PKC?

The catalytic region, also known as the kinase core, is responsible for the enzyme's kinase activity, including binding ATP and the substrate protein, and performing the phosphorylation reaction.

What is the general structural characteristic of the catalytic domain of known protein kinases?

The crystal structures of protein kinases typically show a bilobal structure, with an N-terminal lobe composed of beta sheets and a C-terminal lobe formed by alpha helices. The ATP and substrate binding sites are located in the cleft between these lobes.

What is the significance of phosphorylation for the activity of PKC enzymes?

Phosphorylation of specific sites within the catalytic region, such as the activation loop, turn motif, and hydrophobic motif (in conventional and novel PKCs), is essential for the enzyme's activity and proper function.

What is the role of PDPK1 in the activation cascade of PKC?

PDPK1 (3-phosphoinositide-dependent protein kinase-1) acts as an upstream kinase that initiates the phosphorylation process for PKC activation, specifically by phosphorylating the activation loop.

How does PKC contribute to smooth muscle function in various parts of the body?

PKC activation contributes to contraction in smooth muscle cells found in numerous locations, including the gastrointestinal tract sphincters, iris dilator muscle, urinary sphincter, uterus, seminal tract, vascular tissue, bronchi, and others.

What is the role of PKC in kidney function, specifically in proximal convoluted tubule cells?

In proximal convoluted tubule cells, PKC activation stimulates the sodium-hydrogen exchanger 3 (NHE3) for proton secretion and sodium reabsorption, and also enhances the basolateral Na-K ATPase activity, both processes contributing to sodium reabsorption.

How does PKC influence neuronal function related to learning and memory?

PKC plays a role in learning and memory processes within neurons. Its activation by neurotransmitters like glutamate via NMDA receptors is linked to memory formation.

What is the connection between PKC and the pathology of diabetes mellitus?

PKC enzymes are implicated in vascular complications of diabetes mellitus, particularly those related to hyperglycemia. They contribute to increased vascular permeability, which can lead to tissue damage.

What are some examples of PKC inhibitors mentioned in the text?

The text mentions several PKC inhibitors, including ruboxistaurin, chelerythrine, miyabenol C, myricitrin, gossypol, bryostatin 1, darovasertib, verbascoside, BIM-1, Ro31-8220, and tamoxifen.

Protein Kinase C Wiki: Decoding PKC: Structure, Function, and Regulation of a Key Kinase Family

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What is Protein Kinase C?

Enzyme Family

Protein Kinase C (PKC), identified by the Enzyme Commission number EC 2.7.11.13, represents a critical family of protein kinase enzymes. These enzymes are instrumental in regulating cellular functions through the phosphorylation of serine and threonine residues on target proteins.

Activation Signals

PKC enzymes are typically activated by intracellular signals, most notably increases in diacylglycerol (DAG) or calcium ions (Ca²⁺). This activation positions PKC as a key player in numerous signal transduction cascades within the cell.

Isozyme Diversity

In humans, the PKC family comprises fifteen distinct isozymes. These are broadly categorized into three subfamilies—conventional (cPKC), novel (nPKC), and atypical (aPKC)—based on their specific second messenger requirements for activation, reflecting a sophisticated regulatory network.

Human Isozymes

Conventional (cPKC)

These isoforms require diacylglycerol (DAG), calcium ions (Ca²⁺), and a phospholipid (like phosphatidylserine) for activation. They include PKC-α, PKC-β_I, PKC-β_II, and PKC-γ, encoded by the PRKCA, PRKCB, and PRKCG genes, respectively.

Novel (nPKC)

Requiring DAG but not Ca²⁺ for activation, this group includes PKC-δ, PKC-ε, PKC-η, and PKC-θ, primarily associated with the PRKCD, PRKCE, PRKCH, and PRKCQ genes.

Atypical (aPKC)

These isoforms are unique in that they do not require either Ca²⁺ or DAG for activation, though they do depend on phospholipids. The key members are PKC-ι and PKC-ζ, encoded by PRKCI and PRKCZ.

Related Kinases

The broader PKC superfamily also includes related kinase families such as PKD (PKD1, PKD2, PKD3) and PKN (PK-N1, PK-N2, PK-N3), which exhibit distinct structural and functional characteristics but share evolutionary origins.

Molecular Architecture

Domain Organization

PKC enzymes possess a conserved structure comprising a regulatory domain and a catalytic domain, linked by a hinge region. The catalytic domain, responsible for substrate binding and phosphorylation, exhibits significant conservation across isoforms and with other serine/threonine kinases.

Regulatory Elements

The regulatory domain, located at the amino-terminus, contains key regions for signal integration. The C1 domain binds DAG and phorbol esters, while the C2 domain acts as a Ca²⁺ sensor in conventional PKCs. A pseudosubstrate region within the regulatory domain maintains the enzyme in an inactive state until allosteric signals trigger its release.

Catalytic Core

While the crystal structures of only a few PKC catalytic domains (e.g., PKC theta and iota) are fully elucidated, their general bilobal organization (N-lobe with β-sheets, C-lobe with α-helices) is characteristic of kinases. This structure houses the ATP-binding and substrate-binding sites.

Phosphorylation's Role

Crucial for enzyme viability and activity, PKC isoforms undergo specific phosphorylation events at sites like the activation loop and hydrophobic motif. This post-translational modification, often initiated by kinases like PDPK1, is essential for achieving the correct conformation for catalytic function.

Mechanisms of Activation

Membrane Translocation

Upon receiving activation signals (DAG, Ca²⁺), PKC enzymes translocate to the cell membrane. This localization is facilitated by receptor-for-activated-C-kinase (RACK) proteins, enabling substrate presentation and subsequent enzymatic activity.

Sustained Signaling

PKC is known for its prolonged activation, persisting even after the initial signaling molecules have dissipated. This sustained activity is thought to involve the continuous production of DAG by phospholipases and potentially the involvement of fatty acids, ensuring robust downstream effects.

Microgravity Impact

Interestingly, the process of PKC translocation to the cell membrane is disrupted in microgravity environments. This phenomenon has been linked to the immunodeficiency observed in astronauts, highlighting PKC's role in immune system regulation.

Cellular Functions

Diverse Roles

PKC enzymes are implicated in a wide array of cellular processes. These include modulating receptor desensitization, regulating membrane dynamics, controlling gene transcription, mediating immune responses, influencing cell growth, and playing a role in learning and memory pathways. Their designation as "memory kinases" underscores their importance in neuronal plasticity.

Cell-Type Specificity

The specific functions executed by PKC are highly dependent on the cell type, owing to variations in substrate availability and signaling pathway integration. The table below illustrates some key examples of PKC's diverse effects across different cell types and systems.

Cell Type	Organ/System	Activators (Ligands → GPCRs)	Effects
Smooth muscle cell (GI tract sphincters)	Digestive system	Prostaglandin F_2α → Thromboxanes	Contraction
Smooth muscle cells in: Iris dilator muscle, Urethral sphincter, Uterus, Arrector pili muscles, Ureter, Urinary bladder	Various	Adrenergic agonists → α1 receptor	Contraction
Smooth muscle cells in: Iris constrictor muscle, Ciliary muscle	Sensory system	Acetylcholine → M3 receptor	Contraction
Smooth muscle cell (vascular)	Circulatory system	5-HT → 5-HT2A receptor Adrenergic agonists → α1 receptor	Vasoconstriction
Smooth muscle cell (seminal tract)	Reproductive system	Adrenergic agonists → α1 receptor	Ejaculation
Smooth muscle cell (GI tract)	Digestive system	5-HT → 5-HT2A or 5-HT2B receptor Acetylcholine → M3 receptor	Contraction
Smooth muscle cell (Bronchi)	Respiratory system	5-HT → 5-HT2A receptor Adrenergic agonists → β2 receptor Acetylcholine → M3 and M1 receptor	Bronchoconstriction
Proximal convoluted tubule cell	Kidney	Angiotensin II → AT1 receptor Adrenergic agonists → α1 receptor	Stimulate NHE3 → H⁺ secretion & Na⁺ reabsorption Stimulate basolateral Na-K ATPase → Na⁺ reabsorption
Neurons in autonomic ganglia	Nervous system	Acetylcholine → M1 receptor	EPSP
Neurons in CNS	Nervous system	5-HT → 5-HT2A receptor Glutamate → NMDA receptor	Neuronal excitation (5-HT) Memory (glutamate)
Platelets	Circulatory system	5-HT → 5-HT2A receptor	Aggregation
Ependymal cells (choroid plexus)	Ventricular system	5-HT → 5-HT2C receptor	↑ Cerebrospinal fluid secretion
Heart muscle	Circulatory system	Adrenergic agonists → β1 receptor	Positive ionotropic effect
Serous cells (salivary gland)	Digestive system	Acetylcholine → M1 and M3 receptors Adrenergic agonists → β1 receptor	↑ secretion ↑ salivary potassium levels
Serous cells (lacrimal gland)	Digestive system	Acetylcholine → M3 receptor	↑ secretion
Adipocyte	Digestive system/Endocrine system	Adrenergic agonists → β3 receptor	Glycogenolysis and Gluconeogenesis
Hepatocyte	Digestive system	Adrenergic agonists → α1 receptor
Sweat gland cells	Integumentary system	Adrenergic agonists → β2 receptor	↑ secretion
Parietal cells	Digestive system	Acetylcholine → M3 receptors	↑ Gastric acid secretion
Lymphocyte	Immune system	T-cell receptor B-cell receptor Killer-cell immunoglobulin-like receptor	CARD11/BCL10/MALT1 complex → NF-κB Adaptive immune system
Myelocyte	Immune system	C-type lectin receptors (CLR) (Dectin 1, Mincle)	CARD9/BCL10/MALT1 complex → NF-κB Innate immune system

Implications in Pathology

Cancer Progression

PKC activation by tumor promoters like phorbol esters can lead to increased oncogene expression, potentially driving cancer progression. However, loss-of-function mutations and reduced PKC levels are frequently observed in cancers, suggesting a complex, often tumor-suppressive role for PKC.

Vascular Health

PKC enzymes are significant mediators of vascular permeability. Dysregulation, particularly through hyperglycemia-associated pathways or cigarette smoke exposure, contributes to endothelial injury, tissue damage, and various vascular diseases. Altered PKC signaling can impact junctional protein organization, leading to increased permeability and inflammation.

Targeting PKC: Inhibitors

Therapeutic Potential

Various compounds act as PKC inhibitors, offering potential therapeutic avenues. Ruboxistaurin, for instance, has been investigated for its benefits in peripheral diabetic nephropathy. Natural inhibitors like chelerythrine, myricitrin, and gossypol are also recognized.

Research & Development

Darovasertib, an investigational drug targeting PKC, is currently in efficacy trials for metastatic uveal melanoma. Other notable inhibitors include Verbascoside, BIM-1, Ro31-8220, and Tamoxifen, each with specific research applications or therapeutic investigations.

Modulating PKC: Activators

Natural Compounds

Ingenol mebutate, derived from Euphorbia peplus, is a notable PKC activator approved for treating actinic keratosis. Bryostatin 1, another natural compound, acts as both a PKC inhibitor and activator, with investigations into its use for Alzheimer's disease.

Synthetic Activators

12-O-Tetradecanoylphorbol-13-acetate (PMA or TPA) is a widely used synthetic diacylglycerol mimic that effectively activates classical PKC isoforms. It is often employed in conjunction with ionomycin to provide the calcium signals required for full activation of certain PKC subtypes.

Related Information

Kinase Families

PKC belongs to the broader family of serine/threonine-specific protein kinases (EC 2.7.11-12). Explore related kinase classifications, including non-specific kinases, pyruvate dehydrogenase kinases, MAP kinases, and cyclindependent kinases, to understand the kinase landscape.

Kinases: Serine/threonine-specific protein kinases (EC 2.7.11-12)

Serine/threonine-specific protein kinases (EC 2.7.11.1-EC 2.7.11.20)
Non-specific serine/threonine protein kinases (EC 2.7.11.1)	LATS1 LATS2 MAST1 MAST2 STK38 STK38L CIT ROCK1 SGK SGK2 SGK3 Protein kinase B (AKT1, AKT2, AKT3) Ataxia telangiectasia mutated mTOR EIF-2 kinases (PKR, HRI, EIF2AK3, EIF2AK4) Wee1 (WEE1)
Pyruvate dehydrogenase kinase (EC 2.7.11.2)	PDK1 PDK2 PDK3 PDK4
Dephospho-(reductase kinase) kinase (EC 2.7.11.3)	AMP-activated protein kinase (PRKAA1, PRKAA2, PRKAB1, PRKAB2, PRKAG1, PRKAG2, PRKAG3)
3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring) kinase (EC 2.7.11.4)	BCKDK BCKDHA BCKDHB
(isocitrate dehydrogenase (NADP+)) kinase (EC 2.7.11.5)	IDH2 IDH3A IDH3B IDH3G
(tyrosine 3-monooxygenase) kinase (EC 2.7.11.6)	STK4
Myosin-heavy-chain kinase (EC 2.7.11.7)	Aurora kinase (Aurora A, B, C)
Fas-activated serine/threonine kinase (EC 2.7.11.8)	FASTK STK10
Goodpasture-antigen-binding protein kinase (EC 2.7.11.9)	-
IκB kinase (EC 2.7.11.10)	CHUK IKK2 TBK1 IKBKE IKBKG IKBKAP
cAMP-dependent protein kinase (EC 2.7.11.11)	Protein kinase A (PRKACG, PRKACB, PRKACA, PRKY)
cGMP-dependent protein kinase (EC 2.7.11.12)	Protein kinase G (PRKG1)
Protein kinase C (EC 2.7.11.13)	Protein kinase C (various isoforms) Protein kinase Cζ PKC alpha PRKCB1 PRKCD PRKCE PRKCH PRKCG PRKCI PRKCQ Protein kinase N1 PKN2 PKN3
Rhodopsin kinase (EC 2.7.11.14)	Rhodopsin kinase
Beta adrenergic receptor kinase (EC 2.7.11.15)	Beta adrenergic receptor kinase-1, -2
G-protein coupled receptor kinases (EC 2.7.11.16)	GRK4 GRK5 GRK6
Ca2+/calmodulin-dependent (EC 2.7.11.17)	Ca2+/calmodulin-dependent protein kinases (CAMK1, CAMK2, CAMK4, etc.)
Myosin light-chain kinase (EC 2.7.11.18)	Myosin light-chain kinases (MYLK, MYLK2, etc.)
Phosphorylase kinase (EC 2.7.11.19)	Phosphorylase kinase (PHKA1, PHKB, PHKG1, etc.)
Elongation factor 2 kinase (EC 2.7.11.20)	EEF2K STK19

Serine/threonine-specific protein kinases (EC 2.7.11.21-EC 2.7.11.30)
Polo kinase (EC 2.7.11.21)	PLK1 PLK2 PLK3 PLK4
Cyclin-dependent kinase (EC 2.7.11.22)	CDK1, CDK2, CDK3, CDK4, CDK5, CDK6, CDK7, CDK8, CDK9, CDK10, CDK12, etc.
(RNA-polymerase)-subunit kinase (EC 2.7.11.23)	RPS6KA5, RPS6KA4, P70S6 kinase, etc.
Mitogen-activated protein kinase (EC 2.7.11.24)	ERK, JNK, p38 MAPK families
MAP3K (EC 2.7.11.25)	MAP3K1, MAP3K7, RAF kinases, MLKs, etc.
Tau-protein kinase (EC 2.7.11.26)	TPK1, GSK-3, etc.
(acetyl-CoA carboxylase) kinase (EC 2.7.11.27)	-
Tropomyosin kinase (EC 2.7.11.28)	-
Low-density-lipoprotein receptor kinase (EC 2.7.11.29)	-
Receptor protein serine/threonine kinase (EC 2.7.11.30)	BMP receptors, ACVR1, etc.

Dual-specificity kinases (EC 2.7.12)
MAP2K	MAP2K1, MAP2K2, MAP2K3, MAP2K4, MAP2K5, MAP2K6, MAP2K7

Databases & Resources

Access comprehensive information on PKC through various biological databases and resources. Explore links to EC numbers, CAS registry, IntEnz, BRENDA, ExPASy, KEGG, Pfam, InterPro, PDB structures, Gene Ontology, PubMed, and NCBI for detailed data.

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Decoding PKC

💡 Dive in with Flashcard Learning! 💡

What is Protein Kinase C? ℹ️

🔬 Enzyme Family

⚡ Activation Signals

🧬 Isozyme Diversity

Human Isozymes 👥

A Conventional (cPKC)

B Novel (nPKC)

C Atypical (aPKC)

D Related Kinases

Molecular Architecture 🏗️

🧩 Domain Organization

🔗 Regulatory Elements

🔒 Catalytic Core

💡 Phosphorylation's Role

Mechanisms of Activation 🚀

📍 Membrane Translocation

⏳ Sustained Signaling

🌌 Microgravity Impact

Cellular Functions 🎯

🌐 Diverse Roles

🗂️ Cell-Type Specificity

Implications in Pathology ⚠️

📈 Cancer Progression

🩸 Vascular Health

Targeting PKC: Inhibitors 🚫

💊 Therapeutic Potential

🔬 Research & Development

Modulating PKC: Activators ✅

🌿 Natural Compounds

🧪 Synthetic Activators

Related Information 🔗

📚 Kinase Families

🏛️ Databases & Resources

Teacher's Corner 🧑‍🏫

Edit and Print this course in the Wiki2Web Teacher Studio

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References

📜 References

Feedback & Support 👍

To report an issue with this page, or to find out ways to support the mission, please click here.

Disclaimer ⚠️

📜 Important Notice

Dive in with Flashcard Learning!

What is Protein Kinase C?

Enzyme Family

Activation Signals

Isozyme Diversity

Human Isozymes

Conventional (cPKC)

Novel (nPKC)

Atypical (aPKC)

Related Kinases

Molecular Architecture

Domain Organization

Regulatory Elements

Catalytic Core

Phosphorylation's Role

Mechanisms of Activation

Membrane Translocation

Sustained Signaling

Microgravity Impact

Cellular Functions

Diverse Roles

Cell-Type Specificity

Implications in Pathology

Cancer Progression

Vascular Health

Targeting PKC: Inhibitors

Therapeutic Potential

Research & Development

Modulating PKC: Activators

Natural Compounds

Synthetic Activators

Related Information

Kinase Families

Databases & Resources

Teacher's Corner

True or False?

Test Your Knowledge!

Gamer's Corner

Discover other topics to study!

References

Feedback & Support

Disclaimer

Important Notice