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First published online April 1, 2009

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...and the Golgi gets a skeleton

The membrane skeleton (which contains ankyrin, spectrin, protein 4.1R and other proteins) forms a scaffold on the cytoplasmic side of the plasma membrane in many cell types, and helps to maintain cell shape and plasma-membrane integrity. Interestingly, spectrin and ankyrin have been shown to associate with the Golgi complex – however, it has not been clear whether additional skeleton components are present at the Golgi, or what the role of a putative Golgi-associated membrane skeleton might be. Now, Xiuli An and colleagues (p. 1091) show that a 200 kDa protein 4.1B isoform (4.1B₂₀₀; a hitherto-unknown variant of protein 4.1) associates dynamically with the Golgi complex in MDCK cells and human bronchial epithelial cells (HBEs). The authors report that, when the expression of 4.1B₂₀₀ is knocked down, the structure of the Golgi complex is perturbed. Moreover, in 4.1B₂₀₀-depleted cells, Na⁺/K⁺-ATPase and the tight-junction proteins ZO-1 and ZO-2 all fail to migrate to the plasma membrane. In subconfluent HBEs (which lack tight junctions), ZO-1 and ZO-2 associate with 4.1B₂₀₀ in the perinuclear region. The authors conclude that 4.1B₂₀₀ is a likely component of a Golgi-associated cytoskeleton, and is required for structural integrity of the Golgi and targeting of a subset of membrane proteins.

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Related articles in JCS:

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
JCS 2009 122: 1091-1099. [Abstract] [Full Text]  

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Related articles in JCS Similar articles in this journal Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Search for Related Content Social Bookmarking                         What's this?