Identification of multiple actin-binding sites in cofilin-phosphatase Slingshot-1L.
Slingshot-1L (SSH1L) is a phosphatase that specifically dephosphorylates and activates cofilin, an actin-severing and -depolymerizing protein. SSH1L binds to and is activated by F-actin in vitro, and co-localizes with F-actin in cultured cells. We examined the F-actin-binding activity, F-actin-mediated phosphatase activation, and subcellular distribution of various mutants of SSH1L. We identified three sites involved in F-actin binding of SSH1L: Trp-458 close to the C-terminus of the phosphatase domain, an LHK motif in the N-terminal region, and an LKR motif in the C-terminal region. These sites play unique roles in the control of subcellular localization and F-actin-mediated activation of SSH1L.
Yamamoto
Masahiro
M
Department of Biomolecular Sciences, Graduate School of Life Sciences, Tohoku University, Sendai, Miyagi 980-8578, Japan.
Nagata-Ohashi
Kyoko
K
Ohta
Yusaku
Y
Ohashi
Kazumasa
K
Mizuno
Kensaku
K
D051339:Actin Depolymerizing Factors / Q000378:metabolism*; D000199:Actins / Q000378:metabolism*; D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D001665:Binding Sites; D002460:Cell Line; D004789:Enzyme Activation; D006801:Humans; D009154:Mutation; D010749:Phosphoprotein Phosphatases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D011485:Protein Binding
D051339:Actin Depolymerizing Factors; D000199:Actins; D010749:Phosphoprotein Phosphatases; C484329:SSH1 protein, human