FEBS Letters | |
p80 ROKα binding protein is a novel splice variant of CRMP‐1 which associates with CRMP‐2 and modulates RhoA‐induced neuronal morphology | |
Hall, Christine1  Tan, Ivan2  Ng, Chong Han2  Leung, Thomas2  Ng, Yvonne2  Lim, Louis2  Cheong, Albert2  | |
[1] Department of Molecular Pathogenesis, Institute of Neurology, UCL, 1 Wakefield Street, London WC1N 1PJ, UK;Glaxo-IMCB Group, Institute of Molecular and Cell Biology, 30 Medical Drive, Singapore 117609 | |
关键词: ROKα; CRMP family; RhoA; Neuronal morphology; CRMP; collapsin response mediator protein; ROK; RhoA binding kinase; MLC2; myosin light chain 2; Sema3A; semaphorin 3A; LPA; lipophosphatidic acid; NGF; nerve growth factor; | |
DOI : 10.1016/S0014-5793(02)03736-5 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
Using antibody against the Rho binding domain of ROKα, two neuronal phosphoproteins of 62 and 80 kDa were co-immunoprecipitated from brain extracts. Peptide analysis revealed their identity as collapsin response mediator proteins (CRMPs); p62 was CRMP-2 whereas p80 was a novel splice form of CRMP-1 with an extended N-terminus. p80 CRMP-1 was able to complex with CRMP-2, suggesting that p80 CRMP-1 and CRMP-2 form oligomers. CRMP-2 was the major substrate of ROK. p80 CRMP-1 interacted with the kinase domain of ROKα, resulting in inhibition of the catalytic activity towards other substrates. Over-expression of p80 CRMP-1 and CRMP-2 together counteracted the effects of RhoA on neurite retraction, an effect enhanced by mutation of the ROK phosphorylation site in CRMP-2. p80 CRMP-1 and CRMP-2 may be modulators of RhoA-dependent signaling, through interaction with and regulation of ROKα.
【 授权许可】
Unknown
【 预 览 】
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