The roles of atypical protein kinase Cs (aPKCs) in the nervous system: targets for neuroregeneration?
Dennis Dik-Long Chau
Kwok-Fai Lau
1.School of Life Sciences, The Chinese University of Hong Kong,Hong Kong Special Administrative Region, China2.School of Life Sciences, The Chinese University of Hong Kong,Hong Kong Special Administrative Region, China
摘要：The protein kinase C (PKC) family: PKC family is a subgroup of the AGC serine-threonine kinases that consists of 10 distinct members in mammals (Spitaler and Cantrell, 2004). They all contain a C-terminal catalytic domain that is connected to the N-terminal regulatory domains. PKCs are subdi-vided into three classes according to their structures and activators. The classical/conventional PKC isoforms possess tandem C1 domains that bind to their well-known activators diacylglycerol and phorbol esters and also contain a C2 domain that mediates the binding of Ca2+-sensitive anionic phospholipids. Novel PKC isoforms also contain C1 domains that bind diacylglycerol and a novel C2 domain that does not coordinate Ca2+. Unlike the classical/conventional and novel PKC classes, atypical PKC isoforms (aPKCs) which include PKCζ and PKCι (also known as PKC λ in rodents), contain an atypical C1 domain that has no affinity to diacylglycerol or phor-bol esters. Instead of a C2 domain, a protein binding Phox/Bem domain 1 is located at the N-terminal of the regulatory region. This domain has been shown to control aPKC activity through interactions with protein adaptors at specific locations. In addition, a truncated isoform, namely protein kinase Mζ (PKMζ), is generated in the nervous system through a neuronal-tissue specific alternative transcription start site in PRKCZ gene. Since all the N-terminal regulatory domains are omitted in the alternative transcription, PKMζ functions as a constitutively active form of PKCζ (Figure 1).
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论文发表日期：2020-08-28
在线出版日期：2025-08-15（本平台首次上网日期，不代表文献的发表时间）
页数：2( 1475-1476 )