Journal
MOLECULAR BIOLOGY OF THE CELL
Volume 17, Issue 7, Pages 2869-2881Publisher
AMER SOC CELL BIOLOGY
DOI: 10.1091/mbc.e05-11-1001
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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 zeta) and that the interaction between these proteins is EGF-dependent. We further show that PAK1 is involved in aPKC phosphorylation and that aPKC zeta 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 zeta 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.
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