The Role of the Clathrin Adaptor AP-1: Polarized Sorting and Beyond

Membranes

Fubito Nakatsu²  Koji Hase¹  Hiroshi Ohno³ 

[1] Department of Biochemistry, Faculty of Pharmacy, Keio University, Tokyo 105-8512, Japan; E-Mail:;Department of Cell Biology, Yale University School of Medicine, 295 Congress Avenue, BCMM237, New Haven, CT 06510, USA;RIKEN Center for Integrative Medical Sciences (IMS), Kanagawa 230-0045, Japan; E-Mail:

关键词: AP complex;    μ1B;    clathrin adaptor;    vesicular transport;    sorting signal;    polarized sorting;    epithelial cell;    inflammation;    cancer;   

DOI  :  10.3390/membranes4040747

来源: mdpi

【 摘 要 】

The selective transport of proteins or lipids by vesicular transport is a fundamental process supporting cellular physiology. The budding process involves cargo sorting and vesicle formation at the donor membrane and constitutes an important process in vesicular transport. This process is particularly important for the polarized sorting in epithelial cells, in which the cargo molecules need to be selectively sorted and transported to two distinct destinations, the apical or basolateral plasma membrane. Adaptor protein (AP)-1, a member of the AP complex family, which includes the ubiquitously expressed AP-1A and the epithelium-specific AP-1B, regulates polarized sorting at the trans-Golgi network and/or at the recycling endosomes. A growing body of evidence, especially from studies using model organisms and animals, demonstrates that the AP-1-mediated polarized sorting supports the development and physiology of multi-cellular units as functional organs and tissues (e.g., cell fate determination, inflammation and gut immune homeostasis). Furthermore, a possible involvement of AP-1B in the pathogenesis of human diseases, such as Crohn’s disease and cancer, is now becoming evident. These data highlight the significant contribution of AP-1 complexes to the physiology of multicellular organisms, as master regulators of polarized sorting in epithelial cells.

【 授权许可】

CC BY   
© 2014 by the authors; licensee MDPI, Basel, Switzerland.