Myosin II Regulatory Light Chain as a Novel Substrate for AIM-1, an Aurora/Ipllp-related Kinase from Rat

Maki Murata-Hori; Katsumi Fumoto; Yasuaki Fukuta; Takahiro Iwasaki; Asako Kikuchi; Masaaki Tatsuka; Hiroshi Hosoya

Maki Murata-Hori, Katsumi Fumoto, Yasuaki Fukuta, Takahiro Iwasaki, Asako Kikuchi, Masaaki Tatsuka, Hiroshi Hosoya

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Keywords: AIM-1, cytokinesis, myosin II regulatory light chain (MRLC), myosin light chain kinase (MLCK), phosphorylation

JOURNAL FREE ACCESS

2000 Volume 128 Issue 6 Pages 903-907

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Abstract

Previous studies demonstrated that the phosphorylated myosin II regulatory light chain (MRLC) is localized at the cleavage furrow of dividing cells, suggesting that phosphorylation of MRLC plays an important role in cytokinesis. However, it remains unclear which kinase (s) phosphorylate MRLC during cytokinesis. AIM-1, an Aurora/Ipllprelated kinase from rat, is known as a serine/threonine kinase that is required for cytokinesis. Here we examined the possibility that AIM-1 is a candidate for a kinase that phosphorylates MRLC during cytokinesis. As a result, we showed that AIM-1 monophosphorylated MRLC at Ser 19 using two-dimensional phosphopeptide mapping analysis and several MRLC mutants. Furthermore, AIM-1 was colocalized with monophosphorylated MRLC at the cleavage furrow of dividing cells. We propose here that AIM-1 may participate in monophosphorylation of MRLC during cytokinesis.

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