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

Tomohisa Hatta1, Shun-Ichiro Iemura1,2, Tomokazu Ohishi3

  • 1Molecular Profiling Research Center for Drug Discovery (molprof), National Institute of Advanced Industrial Science and Technology (AIST), 2-3-26 Aomi, Koto-ku, Tokyo, 1345-0064, Japan.

Scientific Reports
|November 15, 2018
PubMed

Insights

Calpain-10 deficiency impacts insulin secretion by altering actin dynamics through MAP1B processing. This suggests a novel mechanism linking calpain-10 to type 2 diabetes mellitus.

Area of Science:

  • Molecular biology
  • Cell biology
  • Endocrinology

Background:

  • Calpain-10 (CAPN10) is a candidate gene for type 2 diabetes mellitus (T2DM).
  • The precise molecular mechanisms underlying CAPN10's role in T2DM remain unclear.

Purpose of the Study:

  • To elucidate the molecular mechanism of calpain-10 in regulating cellular processes relevant to T2DM.
  • To investigate the interaction of CAPN10 with microtubule-associated protein 1 (MAP1) family proteins.

Main Methods:

  • Immunofluorescence analysis of Capn10 knockout mouse embryonic fibroblasts.
  • Fluorescence recovery after photo-bleaching (FRAP) to assess actin dynamics.
  • Analysis of insulin secretion in pancreatic islets from CAPN10 knockout mice.

Main Results:

  • CAPN10 processes MAP1 family proteins, affecting their binding to microtubules and actin filaments.
  • MAP1B localizes to actin filaments in Capn10-deficient cells.
  • Calpain-10 regulates actin dynamics through MAP1B cleavage.
  • CAPN10 deficiency leads to increased insulin secretion in pancreatic islets.

Conclusions:

  • Calpain-10 regulates actin dynamics and reorganization via MAP1 family protein processing.
  • CAPN10 deficiency may influence insulin secretion through altered actin dynamics.
  • These findings provide insights into the molecular basis of T2DM pathogenesis related to CAPN10.

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