Difference between revisions of "Kinase Family PKC"
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[[kinase classification|Kinase Classification]]: [[Kinase_Group_AGC|Group AGC]]: [[Kinase_Family_PKC|Family PKC]] | [[kinase classification|Kinase Classification]]: [[Kinase_Group_AGC|Group AGC]]: [[Kinase_Family_PKC|Family PKC]] | ||
| − | The Protein Kinase C family are second messengers activated by calcium, lipids and DAG. Four major subfamilies are found throughout | + | The Protein Kinase C family are second messengers activated by calcium, lipids and di-acyl glycerol (DAG). Four major subfamilies are found throughout animals, with different accessory domains, activators, and functions. |
====[[Kinase_Subfamily_PKCa|Subfamily PKCa]]==== | ====[[Kinase_Subfamily_PKCa|Subfamily PKCa]]==== | ||
| − | Classical PKCs, activated by Ca2+, DAG and lipids, represented in human by PKC alpha, beta and gamma (PKCα, PKCβ, PKCγ) forms. | + | 'Classical' PKCs, activated by Ca2+, DAG and lipids, represented in human by PKC alpha, beta and gamma (PKCα, PKCβ, PKCγ) forms. |
| − | PKCa members have twin DAG-binding C1 domains, followed by a C2 Ca/phospholipid-binding domain and a | + | PKCa members have twin DAG-binding C1 domains, followed by a C2 Ca/phospholipid-binding domain and a kinase domain. |
====[[Kinase_Subfamily_PKCd|Subfamily PKCd]]==== | ====[[Kinase_Subfamily_PKCd|Subfamily PKCd]]==== | ||
| − | Novel PKCs that are Ca2+-independent, including human PKC delta and theta (PKCd/δ, PKCt/θ) | + | 'Novel' PKCs that are Ca2+-independent, including human PKC delta and theta (PKCd/δ, PKCt/θ) |
| − | Have a specialized C2 domain first, followed by twin C1 domains and then the | + | Have a specialized C2 domain first, followed by twin C1 domains and then the kinase domain. |
====[[Kinase_Subfamily_PKCh|Subfamily PKCh]]==== | ====[[Kinase_Subfamily_PKCh|Subfamily PKCh]]==== | ||
| − | Another subfamily of novel PKCs, including human PKC epsilon (PKCe/ε) and eta (PKCh/η) | + | Another subfamily of 'novel' PKCs, including human PKC epsilon (PKCe/ε) and eta (PKCh/η) |
| − | Like PKCd, PKCh have a specialized C2 domain first, followed by twin C1 domains and then the | + | Like PKCd, PKCh have a specialized C2 domain first, followed by twin C1 domains and then the kinase domain. |
====[[Kinase_Subfamily_PKCi|Subfamily PKCi]]==== | ====[[Kinase_Subfamily_PKCi|Subfamily PKCi]]==== | ||
These are the atypical PKCs activated by phosphatidyl serine, with human members iota and zeta (PKCi/ι, PKCz/ζ). | These are the atypical PKCs activated by phosphatidyl serine, with human members iota and zeta (PKCi/ι, PKCz/ζ). | ||
| − | ====[[Kinase_Subfamily_PKC-fun|Subfamily | + | ====[[Kinase_Subfamily_PKC-fun|Subfamily PKC-fun]]==== |
Fungi typically have a single PKC homolog, with distinct functions and domain structure: triple HR1 domains followed by C2, then kinase domains. The HR1 domains bind the small GTPase Rho, downstream of cell wall stress receptors, and cause activation of a divergent MAPK cascade. | Fungi typically have a single PKC homolog, with distinct functions and domain structure: triple HR1 domains followed by C2, then kinase domains. The HR1 domains bind the small GTPase Rho, downstream of cell wall stress receptors, and cause activation of a divergent MAPK cascade. | ||
Latest revision as of 22:07, 12 November 2021
Kinase Classification: Group AGC: Family PKC
The Protein Kinase C family are second messengers activated by calcium, lipids and di-acyl glycerol (DAG). Four major subfamilies are found throughout animals, with different accessory domains, activators, and functions.
Subfamily PKCa
'Classical' PKCs, activated by Ca2+, DAG and lipids, represented in human by PKC alpha, beta and gamma (PKCα, PKCβ, PKCγ) forms. PKCa members have twin DAG-binding C1 domains, followed by a C2 Ca/phospholipid-binding domain and a kinase domain.
Subfamily PKCd
'Novel' PKCs that are Ca2+-independent, including human PKC delta and theta (PKCd/δ, PKCt/θ) Have a specialized C2 domain first, followed by twin C1 domains and then the kinase domain.
Subfamily PKCh
Another subfamily of 'novel' PKCs, including human PKC epsilon (PKCe/ε) and eta (PKCh/η) Like PKCd, PKCh have a specialized C2 domain first, followed by twin C1 domains and then the kinase domain.
Subfamily PKCi
These are the atypical PKCs activated by phosphatidyl serine, with human members iota and zeta (PKCi/ι, PKCz/ζ).
Subfamily PKC-fun
Fungi typically have a single PKC homolog, with distinct functions and domain structure: triple HR1 domains followed by C2, then kinase domains. The HR1 domains bind the small GTPase Rho, downstream of cell wall stress receptors, and cause activation of a divergent MAPK cascade.
Gerard 01:45, 12 April 2018 (UTC)
