The HNF-1 target collectrin controls insulin exocytosis by SNARE complex formation

Cell Metab. 2005 Dec;2(6):373-84. doi: 10.1016/j.cmet.2005.11.003.

Abstract

Defective glucose-stimulated insulin secretion is the main cause of hyperglycemia in type 2 diabetes mellitus. Mutations in HNF-1alpha cause a monogenic form of type 2 diabetes, maturity-onset diabetes of the young (MODY), characterized by impaired insulin secretion. Here we report that collectrin, a recently cloned kidney-specific gene of unknown function, is a target of HNF-1alpha in pancreatic beta cells. Expression of collectrin was decreased in the islets of HNF-1alpha (-/-) mice, but was increased in obese hyperglycemic mice. Overexpression of collectrin in rat insulinoma INS-1 cells or in the beta cells of transgenic mice enhanced glucose-stimulated insulin exocytosis, without affecting Ca(2+) influx. Conversely, suppression of collectrin attenuated insulin secretion. Collectrin bound to SNARE complexes by interacting with snapin, a SNAP-25 binding protein, and facilitated SNARE complex formation. Therefore, collectrin is a regulator of SNARE complex function, which thereby controls insulin exocytosis.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Base Sequence
  • Blotting, Northern
  • Calcium / metabolism
  • Cell Line
  • Cloning, Molecular
  • DNA, Complementary / metabolism
  • Diabetes Mellitus, Type 2 / metabolism*
  • Disease Models, Animal
  • Exocytosis
  • Genes, Reporter
  • Glucose / chemistry
  • Glucose / metabolism
  • Glutathione Transferase / metabolism
  • Growth Hormone / metabolism
  • Hepatocyte Nuclear Factor 1 / metabolism*
  • Humans
  • Immunoblotting
  • Immunohistochemistry
  • Immunoprecipitation
  • Insulin / metabolism
  • Insulin Secretion
  • Insulin-Secreting Cells / metabolism
  • Insulinoma
  • Islets of Langerhans / cytology
  • Membrane Glycoproteins / metabolism*
  • Mice
  • Mice, Transgenic
  • Microscopy, Fluorescence
  • Microscopy, Immunoelectron
  • Models, Genetic
  • Molecular Sequence Data
  • Nucleic Acid Hybridization
  • Oligonucleotide Array Sequence Analysis
  • Pancreas / metabolism
  • Photons
  • Protein Binding
  • RNA, Messenger / metabolism
  • RNA, Small Interfering / metabolism
  • Rats
  • Reverse Transcriptase Polymerase Chain Reaction
  • SNARE Proteins / metabolism*
  • Time Factors
  • Tissue Distribution
  • Transcription, Genetic
  • Two-Hybrid System Techniques

Substances

  • CLTRN protein, human
  • DNA, Complementary
  • Insulin
  • Membrane Glycoproteins
  • RNA, Messenger
  • RNA, Small Interfering
  • SNARE Proteins
  • Hepatocyte Nuclear Factor 1
  • Growth Hormone
  • Glutathione Transferase
  • Glucose
  • Calcium