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MBC in Press, published online ahead of print February 9, 2005
Mol. Biol. Cell 10.1091/mbc.E04-07-0554

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Submitted on July 6, 2004
Accepted on January 24, 2005

Phosphorylation Controls CLIMP-63-mediated Anchoring of the Endoplasmic Reticulum to Microtubules

Cécile Vedrenne, Dieter R. Klopfenstein,* and Hans-Peter Hauri

Biozentrum, University of Basel, CH-4056 Basel, Switzerland

Monitoring Editor: Jennifer Lippincott-Schwartz

The microtubule-binding protein CLIMP-63 is an integral membrane protein that links the endoplasmic reticulum (ER) to microtubules. Here we tested if this interaction is regulated by phosphorylation. Metabolic labeling with 32P showed that CLIMP-63 is a phosphoprotein with increased phosphorylation during mitosis. CLIMP-63 of mitotic cells is unable to bind to microtubules in vitro. Mitotic phosphorylation can be prevented by mutation of serines 3, 17 and 19 in the cytoplasmic domain of CLIMP-63. When these residues are mutated to glutamic acid, and hence mimic mitotic phosphorylation, CLIMP-63 does no longer bind to microtubules in vitro. Overexpression of the phospho-mimicking mitotic form of CLIMP-63 in interphase cells leads to a collapse of the ER around the nucleus leaving the microtubular network intact. The results suggest that CLIMP-63-mediated stable anchoring of the ER to microtubules is required to maintain the spatial distribution of the ER during interphase and that this interaction is abolished by phosphorylation of CLIMP-63 during mitosis.

*Present address: Center for Molecular Physiology of the Brain, Georg August University, D-37073 Göttingen, Germany.

Address correspondence to: Hans-Peter Hauri (Hans-Peter.Hauri{at}unibas.ch)






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