Phosphorylation controls CLIMP-63-mediated anchoring of the endoplasmic reticulum to microtubules

Vedrenne, C. and Klopfenstein, D. R. and Hauri, H. -P.. (2005) Phosphorylation controls CLIMP-63-mediated anchoring of the endoplasmic reticulum to microtubules. Molecular Biology of the Cell, 16 (4). pp. 1928-1937.

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Official URL: http://edoc.unibas.ch/dok/A5257748

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The microtubule-binding 63-kDa cytoskeleton-linking membrane protein (CLIMP-63) is an integral membrane protein that links the endoplasmic reticulum (ER) to microtubules. Here, we tested whether this interaction is regulated by phosphorylation. Metabolic labeling with (32)P 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.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Former Organization Units Biozentrum > Pharmacology/Neurobiology (Hauri)
UniBasel Contributors:Hauri, Hans-Peter
Item Type:Article, refereed
Article Subtype:Research Article
Publisher:American Society for Cell Biology
Note:Publication type according to Uni Basel Research Database: Journal article
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Last Modified:07 Nov 2017 08:09
Deposited On:22 Mar 2012 13:18

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