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First published online 19 March 2009
doi: 10.1242/jcs.039644

Journal of Cell Science 122, 1091-1099 (2009)
Published by The Company of Biologists 2009
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Research Article

A Golgi-associated protein 4.1B variant is required for assimilation of proteins in the membrane

Qiaozhen Kang*, Ting Wang, Huizheng Zhang, Narla Mohandas and Xiuli An{ddagger}

Red Cell Physiology Laboratory, New York Blood Center, New York, NY 10065, USA

{ddagger} Author for correspondence (e-mail: xan{at}nybloodcenter.org)

Accepted 2 December 2008

The archetypal membrane skeleton is that of the erythrocyte, consisting predominantly of spectrin, actin, ankyrin R and protein 4.1R. The presence in the Golgi of a membrane skeleton with a similar structure has been inferred, based on the identification of Golgi-associated spectrin and ankyrin. It has long been assumed that a Golgi-specific protein 4.1 must also exist, but it has not previously been found. We demonstrate here that a hitherto unknown form of protein 4.1, a 200 kDa 4.1B, is associated with the Golgi of Madin-Darby canine kidney (MDCK) and human bronchial epithelial (HBE) cells. This 4.1B variant behaves like a Golgi marker after treatment with Brefeldin A and during mitosis. Depletion of the protein in HBE cells by siRNA resulted in disruption of the Golgi structure and failure of Na+/K+-ATPase, ZO-1 and ZO-2 to migrate to the membrane. Thus, this newly identified Golgi-specific protein 4.1 appears to have an essential role in maintaining the structure of the Golgi and in assembly of a subset of membrane proteins.

Key words: Golgi, Cytoskeleton, Protein 4.1B, Spectrin


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[Abstract] [Full Text] [PDF]


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