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Journal of Cell Science 115, 2031-2040 (2002)
© 2002 The Company of Biologists Limited

Research Article

Integrin clustering induces kinectin accumulation

Huan Tran1, Roumen Pankov1, Simon D. Tran1, Brian Hampton2, Wilson H. Burgess2 and Kenneth M. Yamada1,*

1 Craniofacial Developmental Biology and Regeneration Branch, National Institute of Dental and Craniofacial Research, National Institutes of Health, Bethesda, MD 20892-4370, USA
2 Department of Tissue Biology, Jerome H. Holland Laboratory, American Red Cross, Rockville, MD 20855, USA

* Author for correspondence (e-mail: kenneth.yamada{at}nih.gov )

Accepted 19 February 2002

Integrin receptors mediate the formation of adhesion complexes and play important roles in signal transduction from the extracellular matrix. Integrin-based adhesion complexes (IAC) contain proteins that link integrins to the cytoskeleton and recruit signaling molecules, including vinculin, paxillin, focal adhesion kinase, talin and {alpha}-actinin. In this study, we describe a ~160 kDa protein that is markedly enriched at IAC induced by clustering integrins with fibronectin-coated beads. Protein sequence analysis reveals that this ~160 kDa protein is kinectin. Kinectin is an integral membrane protein found in endoplasmic reticulum, and it serves as a receptor for the motor protein kinesin. Fibronectin-induced IAC sequestered over half of the total cellular content of kinectin within 20 minutes. In addition, two other ER-resident proteins, RAP [low-density lipoprotein receptor-related protein (LRP) receptor-associated protein] and calreticulin, were found to be clustered at IAC, whereas kinesin was not. Our results identify a novel class of constituents of IAC.

Key words: Adhesion, Integrin, Kinectin, Kinesin-binding proteins, Endoplasmic reticulum, Fibronectin




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© The Company of Biologists Ltd 2002