Shin Choonshik, Ahn Joong-Hoon, Lim Yoongho
Bio/Molecular Informatics Center, Konkuk University, Seoul 143-701, Republic of Korea.
Biochem Biophys Res Commun. 2005 Nov 11;337(1):154-9. doi: 10.1016/j.bbrc.2005.08.270.
One of protein kinase C (PKC) isozymes, PKC beta binds to receptor for activated C kinase 1 (RACK1), and their complex is suggested to be translocated to melanosomes. The binding site of PKC beta for RACK1 is considered one of its catalytic domains, V5 domain which consists of three motifs such as V5-1, V5-2, and V5-3. Among these, V5-1 region, extreme C-terminal residues of PKC beta showed the highest RACK1-binding affinity. PKC beta can be classified into PKC betaI and PKC betaII based on their different V5 domains. RACK1-binding affinity of PKC betaII is five times greater than that of PKC betaI. The structures of PKC betaI, PKC betaII, and RACK1 are not known. However, the conformational study on PKC betaII V5-1 region showing high RACK1-binding selectivity may help us in understanding the interaction between RACK1 and PKC betaII.
蛋白激酶C(PKC)同工酶之一的PKCβ与活化C激酶1受体(RACK1)结合,并且它们的复合物被认为会转位至黑素小体。PKCβ与RACK1的结合位点被认为是其催化结构域之一,即V5结构域,它由V5-1、V5-2和V5-3三个基序组成。其中,PKCβ的极端C末端残基V5-1区域显示出最高的RACK1结合亲和力。基于不同的V5结构域,PKCβ可分为PKCβI和PKCβII。PKCβII与RACK1的结合亲和力比PKCβI高五倍。PKCβI、PKCβII和RACK1的结构尚不清楚。然而,对显示出高RACK1结合选择性的PKCβII V5-1区域进行构象研究可能有助于我们理解RACK1与PKCβII之间的相互作用。