Calpain-10 regulates actin dynamics by proteolysis of microtubule-associated protein 1B

Tomohisa Hatta, Shun ichiro Iemura, Tomokazu Ohishi, Hiroshi Nakayama, Hiroyuki Seimiya, Takao Yasuda, Katsumi Iizuka, Mitsunori Fukuda, Jun Takeda, Tohru Natsume, Yukio Horikawa

Research output: Contribution to journalArticlepeer-review

4 Citations (Scopus)

Abstract

Calpain-10 (CAPN10) is the calpain family protease identified as the first candidate susceptibility gene for type 2 diabetes mellitus (T2DM). However, the detailed molecular mechanism has not yet been elucidated. Here we report that CAPN10 processes microtubule associated protein 1 (MAP1) family proteins into heavy and light chains and regulates their binding activities to microtubules and actin filaments. Immunofluorescent analysis of Capn10−/− mouse embryonic fibroblasts shows that MAP1B, a member of the MAP1 family of proteins, is localized at actin filaments rather than at microtubules. Furthermore, fluorescence recovery after photo-bleaching analysis shows that calpain-10 regulates actin dynamics via MAP1B cleavage. Moreover, in pancreatic islets from CAPN10 knockout mice, insulin secretion was significantly increased both at the high and low glucose levels. These findings indicate that deficiency of calpain-10 expression may affect insulin secretion by abnormal actin reorganization, coordination and dynamics through MAP1 family processing.

Original languageEnglish
Article number16756
JournalScientific reports
Volume8
Issue number1
DOIs
Publication statusPublished - 2018 Dec 1

ASJC Scopus subject areas

  • General

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