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A novel direct interaction of endoplasmic reticulum with microtubules
JournalArticle (Originalarbeit in einer wissenschaftlichen Zeitschrift)
 
ID 153373
Author(s) Klopfenstein, D R; Kappeler, F; Hauri, H P
Author(s) at UniBasel Hauri, Hans-Peter
Year 1998
Title A novel direct interaction of endoplasmic reticulum with microtubules
Journal The EMBO journal
Volume 17
Number 21
Pages / Article-Number 6168-77
Keywords cytoskeleton, endoplasmic reticulum, linker protein, microtubules, p63
Abstract The positioning and dynamics of organelles in eukaryotic cells critically depend on membrane-cytoskeleton interactions. Motor proteins play an important role in the directed movement of organelle membranes along microtubules, but the basic mechanism by which membranes stably interact with the microtubule cytoskeleton is largely unknown. Here we report that p63, an integral membrane protein of the reticular subdomain of the rough endoplasmic reticulum (ER), binds microtubules in vivo and in vitro. Overexpression of p63 in cell culture led to a striking rearrangement of the ER and to concomitant bundling of microtubules along the altered ER. Mutational analysis of the cytoplasmic domain of p63 revealed two determinants responsible for these changes: an ER rearrangement determinant near the N-terminus and a central microtubule-binding region. The two determinants function independently of one another as indicated by deletion experiments. A peptide corresponding to the cytoplasmic tail of p63 promoted microtubule polymerization in vitro. p63 is the first identified integral membrane protein that can link a membrane organelle directly to microtubules. By doing so, it may contribute to the positioning of the ER along microtubules.
Publisher Nature Publishing Group
ISSN/ISBN 0261-4189
edoc-URL http://edoc.unibas.ch/dok/A5257776
Full Text on edoc No
Digital Object Identifier DOI 10.1093/emboj/17.21.6168
PubMed ID http://www.ncbi.nlm.nih.gov/pubmed/9799226
ISI-Number WOS:000076984900007
Document type (ISI) Journal Article
 
   

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