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Vol. 17, Issue 7, 2869-2881, July 2006
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Regulate Myosin II-B Phosphorylation: A Novel Signaling Pathway Regulating Filament Assembly
Department of Biochemistry, Institute of Medical Sciences, Faculty of Medicine, The Hebrew University, Jerusalem 91120, Israel
Submitted November 2, 2005;
Revised March 28, 2006;
Accepted April 5, 2006
Monitoring Editor: Martin A. Schwartz
Many signaling pathways regulate the function of the cellular cytoskeleton. Yet we know very little about the proteins involved in the cross-talk between the signaling and the cytoskeletal systems. Here we show that myosin II-B, an important cytoskeletal protein, resides in a complex with p21-activated kinase 1 (PAK1) and atypical protein kinase C (PKC) zeta (aPKC
) and that the interaction between these proteins is EGF-dependent. We further show that PAK1 is involved in aPKC phosphorylation and that aPKC phosphorylates myosin II-B directly on a specific serine residue in an EGF-dependent manner. This latter phosphorylation is specific to isoform B of myosin II, and it leads to slower filament assembly of myosin II-B. Furthermore, a decrease in aPKC expression in the cells alters myosin II-B cellular organization. Our finding of a new signaling pathway involving PAK1, aPKC, and myosin II-B, which is implicated in myosin II-B filament assembly and cellular organization, provides an important link between the signaling system and cytoskeletal dynamics.
Address correspondence to: Shoshana Ravid ( ravid{at}cc.huji.ac.il)
Abbreviations used: PAK1, p21-activated kinase 1; aPKC, atypical PKC zeta; MLC, myosin light chain; NMHC, non-muscle myosin II heavy chain; IP-PAK1, immunoprecipitated PAK1; CKII, casein kinase II.
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