Dynamin is functionally coupled to insulin granule exocytosis

Le Min, Yuk M. Leung, Alejandra Tomas, Robert T. Watson, Herbert Y. Gaisano, Philippe A. Halban, Jeffrey E. Pessin, June Chunqiu Hou

Research output: Contribution to journalArticlepeer-review

35 Scopus citations


The insulin granule integral membrane protein marker phogrin-green fluorescent protein was co-localized with insulin in Min6B1 β-cell secretory granules but did not undergo plasma membrane translocation following glucose stimulation. Surprisingly, although expression of a dominant-interfering dynamin mutant (Dyn/K44A) inhibited transferrin receptor endocytosis, it had no effect on phogringreen fluorescent protein localization in the basal or secretagogue-stimulated state. By contrast, co-expression of Dyn/K44A with human growth hormone as an insulin secretory marker resulted in a marked inhibition of human growth hormone release by glucose, KCl, and a combination of multiple secretagogues. Moreover, serial pulse depolarization stimulated an increase in cell surface capacitance that was also blocked in cells expressing Dyn/K44A. Similarly, small interference RNA-mediated knockdown of dynamin resulted in marked inhibition of glucose-stimulated insulin secretion. Together, these data suggest the presence of a selective kiss and run mechanism of insulin release. Moreover, these data indicate a coupling between endocytosis and exocytosis in the regulation of β-cell insulin secretion.

Original languageEnglish (US)
Pages (from-to)33530-33536
Number of pages7
JournalJournal of Biological Chemistry
Issue number46
StatePublished - Nov 16 2007
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology


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