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Journal articles
Tubulin tyrosination is a major factor affecting the recruitment of CAP-Gly proteins at microtubule plus ends.
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.
Cited literature [46 references]
https://www.hal.inserm.fr/inserm-00380096
Contributor : Annie Andrieux <>
Submitted on : Wednesday, May 6, 2009 - 11:11:34 AM
Last modification on : Monday, December 14, 2020 - 10:22:03 AM
Long-term archiving on: : Thursday, June 10, 2010 - 6:46:20 PM
Contributor : Annie Andrieux <>
Submitted on : Wednesday, May 6, 2009 - 11:11:34 AM
Last modification on : Monday, December 14, 2020 - 10:22:03 AM
Long-term archiving on: : Thursday, June 10, 2010 - 6:46:20 PM
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Lety_JCB_2006_submit_file.pdf
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