Tubulin tyrosination is a major factor affecting the recruitment of CAP-Gly proteins at microtubule plus ends.

2.50
Hdl Handle:
http://hdl.handle.net/10033/13782
Title:
Tubulin tyrosination is a major factor affecting the recruitment of CAP-Gly proteins at microtubule plus ends.
Authors:
Peris, Leticia; Thery, Manuel; Fauré, Julien; Saoudi, Yasmina; Lafanechère, Laurence; Chilton, John K; Gordon-Weeks, Phillip; Galjart, Niels; Bornens, Michel; Wordeman, Linda; Wehland, Juergen; Andrieux, Annie; Job, Didier
Abstract:
Tubulin-tyrosine ligase (TTL), the enzyme that catalyzes the addition of a C-terminal tyrosine residue to alpha-tubulin in the tubulin tyrosination cycle, is involved in tumor progression and has a vital role in neuronal organization. We show that in mammalian fibroblasts, cytoplasmic linker protein (CLIP) 170 and other microtubule plus-end tracking proteins comprising a cytoskeleton-associated protein glycine-rich (CAP-Gly) microtubule binding domain such as CLIP-115 and p150 Glued, localize to the ends of tyrosinated microtubules but not to the ends of detyrosinated microtubules. In vitro, the head domains of CLIP-170 and of p150 Glued bind more efficiently to tyrosinated microtubules than to detyrosinated polymers. In TTL-null fibroblasts, tubulin detyrosination and CAP-Gly protein mislocalization correlate with defects in both spindle positioning during mitosis and cell morphology during interphase. These results indicate that tubulin tyrosination regulates microtubule interactions with CAP-Gly microtubule plus-end tracking proteins and provide explanations for the involvement of TTL in tumor progression and in neuronal organization.
Citation:
J. Cell Biol. 2006, 174(6):839-49
Issue Date:
11-Sep-2006
URI:
http://hdl.handle.net/10033/13782
DOI:
10.1083/jcb.200512058
PubMed ID:
16954346
Type:
Article
Language:
en
ISSN:
0021-9525
Appears in Collections:
Publications of Dept. Cell Biology (ZB)

Full metadata record

DC FieldValue Language
dc.contributor.authorPeris, Leticia-
dc.contributor.authorThery, Manuel-
dc.contributor.authorFauré, Julien-
dc.contributor.authorSaoudi, Yasmina-
dc.contributor.authorLafanechère, Laurence-
dc.contributor.authorChilton, John K-
dc.contributor.authorGordon-Weeks, Phillip-
dc.contributor.authorGaljart, Niels-
dc.contributor.authorBornens, Michel-
dc.contributor.authorWordeman, Linda-
dc.contributor.authorWehland, Juergen-
dc.contributor.authorAndrieux, Annie-
dc.contributor.authorJob, Didier-
dc.date.accessioned2007-09-25T08:25:17Z-
dc.date.available2007-09-25T08:25:17Z-
dc.date.issued2006-09-11-
dc.identifier.citationJ. Cell Biol. 2006, 174(6):839-49en
dc.identifier.issn0021-9525-
dc.identifier.pmid16954346-
dc.identifier.doi10.1083/jcb.200512058-
dc.identifier.urihttp://hdl.handle.net/10033/13782-
dc.description.abstractTubulin-tyrosine ligase (TTL), the enzyme that catalyzes the addition of a C-terminal tyrosine residue to alpha-tubulin in the tubulin tyrosination cycle, is involved in tumor progression and has a vital role in neuronal organization. We show that in mammalian fibroblasts, cytoplasmic linker protein (CLIP) 170 and other microtubule plus-end tracking proteins comprising a cytoskeleton-associated protein glycine-rich (CAP-Gly) microtubule binding domain such as CLIP-115 and p150 Glued, localize to the ends of tyrosinated microtubules but not to the ends of detyrosinated microtubules. In vitro, the head domains of CLIP-170 and of p150 Glued bind more efficiently to tyrosinated microtubules than to detyrosinated polymers. In TTL-null fibroblasts, tubulin detyrosination and CAP-Gly protein mislocalization correlate with defects in both spindle positioning during mitosis and cell morphology during interphase. These results indicate that tubulin tyrosination regulates microtubule interactions with CAP-Gly microtubule plus-end tracking proteins and provide explanations for the involvement of TTL in tumor progression and in neuronal organization.en
dc.format.extent2891464 bytes-
dc.format.mimetypeapplication/pdf-
dc.language.isoenen
dc.titleTubulin tyrosination is a major factor affecting the recruitment of CAP-Gly proteins at microtubule plus ends.en
dc.typeArticleen
dc.format.digYES-

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