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

@article{citeulike:2234603, 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.}, address = {Laboratoire du Cytosquelette, Institut National de la Sant\'{e} et de la Recherche M\'{e}dicale U366, D\'{e}partement R\'{e}ponse et Dynamique Cellulaire, Commisariat \`{a} l'Energie Atomique Grenoble, 38054 Grenoble, France.}, author = {Peris, L. and Thery, M. and Faur\'{e}, J. and Saoudi, Y. and Lafanech\`{e}re, L. and Chilton, J. K. and Gordon-Weeks, P. and Galjart, N. and Bornens, M. and Wordeman, L. and Wehland, J. and Andrieux, A. and Job, D. }, citeulike-article-id = {2234603}, comment = {Manuel's micropatterns in Fig. 8}, doi = {10.1083/jcb.200512058}, issn = {0021-9525}, journal = {J Cell Biol}, keywords = {adhesion, cell\_culture, centrosome, cytosqueleton, micropatterns, microtubules, tips}, month = {September}, number = {6}, pages = {839--849}, posted-at = {2008-01-15 10:59:18}, priority = {0}, title = {Tubulin tyrosination is a major factor affecting the recruitment of CAP-Gly proteins at microtubule plus ends.}, url = {http://dx.doi.org/10.1083/jcb.200512058}, volume = {174}, year = {2006} }

TY - JOUR ID - citeulike:2234603 L3 - citeulike-article-id:2234603 TI - Tubulin tyrosination is a major factor affecting the recruitment of CAP-Gly proteins at microtubule plus ends. JF - J Cell Biol VL - 174 IS - 6 SP - 839 EP - 849 AD - Laboratoire du Cytosquelette, Institut National de la Santé et de la Recherche Médicale U366, Département Réponse et Dynamique Cellulaire, Commisariat à l'Energie Atomique Grenoble, 38054 Grenoble, France. SN - 0021-9525 N2 - 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. KW - adhesion KW - cell_culture KW - centrosome KW - cytosqueleton KW - micropatterns KW - microtubules KW - tips N1 - Manuel's micropatterns in Fig. 8 AU - Peris, L AU - Thery, M AU - Fauré, J AU - Saoudi, Y AU - Lafanechère, L AU - Chilton, JK AU - Gordon-Weeks, P AU - Galjart, N AU - Bornens, M AU - Wordeman, L AU - Wehland, J AU - Andrieux, A AU - Job, D PY - 2006/09/11/ UR - http://dx.doi.org/10.1083/jcb.200512058 ER -