p21-activated kinase PAK phosphorylates desmin at sites different from those for Rho-associated kinase.

Abstract:

:p21-activated kinase (PAK) and Rho-associated kinase (Rho-kinase) have been shown to induce Ca(2+)-independent contraction of smooth muscle. PAK-induced contraction of Triton-skinned smooth muscle correlates with increased phosphorylation of caldesmon and desmin, although the role of desmin phosphorylation has remained obscure. Here we report that desmin serves as an excellent substrate for PAK in vitro. PAK phosphorylated desmin in a GTP. Cdc42/Rac-dependent manner. Phosphorylation of desmin by PAK dramatically inhibited its filament-forming ability. PAK phosphorylated mainly serine residues of the head domain of desmin, and the major phosphorylation sites differed from those for Rho-kinase. These results suggest that different site-specific phosphorylation of desmin via two divergent protein kinases downstream of Rho family GTPases would seem to increase the regulatory potential for organization of desmin filaments.

authors

Ohtakara K,Inada H,Goto H,Taki W,Manser E,Lim L,Izawa I,Inagaki M

doi

10.1006/bbrc.2000.2854

subject

Has Abstract

pub_date

2000-06-16 00:00:00

pages

712-6

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(00)92854-7

journal_volume

272

pub_type

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