HAP1 helps to regulate actin-based transport of insulin-containing granules in pancreatic β cells

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• 作者：Zhiyong Wang ; Ting Peng ; Hongnian Wu ; Jun He ; He Li
• 关键词：Huntingtin ; associated protein 1 ; Insulin ; Myosin ; Phogrin ; Transport
• 刊名：Histochemistry and Cell Biology
• 出版年：2015
• 出版时间：July 2015
• 年：2015
• 卷：144
• 期：1
• 页码：39-48
• 全文大小：1,753 KB
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• 作者单位：Zhiyong Wang (1) (2)
  Ting Peng (1)
  Hongnian Wu (1)
  Jun He (1)
  He Li (1)
  
  1. Division of Histology and Embryology, Department of Anatomy, Tongji Medical College, Huazhong University of Science and Technology, Wuhan, 430030, People’s Republic of China
  2. Department of Anatomy, Xinxiang Medical University, Xinxiang, 453003, People’s Republic of China
  
• 刊物类别：Medicine
• 刊物主题：Medicine & Public Health
  Anatomy
  Medicine/Public Health, general
  
• 出版者：Springer Berlin / Heidelberg
• ISSN：1432-119X

文摘

Huntingtin-associated protein 1 (HAP1) is enriched in neurons and binds to polyglutamine-expanded huntingtin. It?consists of two alternatively spliced isoforms, HAP1A and HAP1B, which differ only in their short C-terminal sequences. Both HAP1A and HAP1B have been also detected in pancreatic β cells, where the loss of HAP1 impairs glucose-stimulated insulin secretion. Here, we use time-lapse laser scanning confocal microscopy to provide direct evidence that HAP1A, but not HAP1B, co-localizes and co-migrates with insulin-containing vesicles and actin-based myosin Va motor protein in the INS-1 pancreatic β cell line. Knocking down HAP1 expression using small interfering RNA significantly inhibited actin-based transport of insulin vesicles following glucose stimulation. Co-immunoprecipitation experiments demonstrated interaction between HAP1A, myosin Va, and phogrin, a transmembrane protein in insulin-containing vesicles. Stimulating INS-1 cells with glucose increased the association of HAP1A with myosin Va, while silencing HAP1 expression reduced the association of myosin Va with phogrin after glucose stimulation, without affecting levels of myosin Va or actin. Our results provide real-time evidence in living cells that HAP1 may help regulate transport of insulin-containing secretory granules along cortical actin filaments. This also raises the possibility that HAP1 may play an important role in actin-based secretory vesicle trafficking in neurons.