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Functional characterization of the microtubule-binding and -destabilizing domains of CPAP and d-SAS-4.

Abstract：

:We previously identified a novel centrosomal protein CPAP, which carries a 112-residue motif that is essential for microtubule destabilization. In this report, we define both the microtubule (MT) binding and destabilizing domains in human CPAP and analyze the mutations that affect its MT-destabilizing activity. Analysis of a series of CPAP truncated proteins showed that the MT-binding domain (MBD; residues 423-607) of CPAP is located next to its MT-destabilizing domain (MDD; residues 311-422). Site-specific mutagenesis revealed that the mutations that either disrupt the alpha-helical structure (Y341P, I346P, L348P, and triple-P) or alter the charge property (KR377EE) of the MDD significantly affect its MT-destabilizing ability. The activity for binding to a tubulin heterodimer was also significantly reduced in KR377EE mutant. Furthermore, we have analyzed the putative function of Drosophila d-SAS-4, a distant relative of human CPAP, which shares a conserved approximately 20-aa sequence with the MDD of CPAP. Our results show that mutations in this conserved sequence also eliminate d-SAS-4's MT-destabilizing activity, suggesting that d-SAS-4 and CPAP may play similar roles within cells.

journal_name

Exp Cell Res

journal_title

Experimental cell research

authors

Hsu WB,Hung LY,Tang CJ,Su CL,Chang Y,Tang TK

doi

10.1016/j.yexcr.2008.05.012

subject

Has Abstract

pub_date

2008-08-15 00:00:00

pages

2591-602

issue

14

eissn

0014-4827

issn

1090-2422

pii

S0014-4827(08)00206-1

journal_volume

314

pub_type

杂志文章

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