000089334 001__ 89334
000089334 005__ 20190316233820.0
000089334 0247_ $$2doi$$a10.1016/S0960-9822(03)00582-7
000089334 037__ $$aARTICLE
000089334 245__ $$aTAC-1 and ZYG-9 form a complex that promotes microtubule assembly in C. elegans embryos
000089334 269__ $$a2003
000089334 260__ $$c2003
000089334 336__ $$aJournal Articles
000089334 500__ $$aSwiss Institute for Experimental Cancer Research (ISREC), CH-1066, Epalinges/Lausanne, Switzerland. 0960-9822 (Print) Journal Article
000089334 520__ $$aBACKGROUND: Modulation of microtubule dynamics is crucial for proper cell division. While a large body of work has made important contributions to our understanding of the mechanisms governing microtubule dynamics in vitro, much remains to be learned about how these mechanisms operate in vivo. RESULTS: We identified TAC-1 as the sole TACC (Transforming Acidic Coiled Coil) protein in C. elegans. TAC-1 consists essentially of a TACC domain, in contrast to the much larger members of this protein family in other species. We find that tac-1 is essential for pronuclear migration and spindle elongation in one-cell-stage C. elegans embryos. Using an in vivo FRAP-based assay, we establish that inactivation of tac-1 results in defective microtubule assembly. TAC-1 is present in the cytoplasm and is enriched at centrosomes in a cell cycle-dependent manner. Centrosomal localization is independent of microtubules but requires the activity of gamma-tubulin and the Aurora-A kinase AIR-1. By conducting FRAP analysis in embryos expressing GFP-TAC-1, we find that centrosomal TAC-1 exchanges rapidly with the cytoplasmic pool. Importantly, we establish that TAC-1 physically interacts with ZYG-9, a microtubule-associated protein (MAP) of the XMAP215 family, both in vitro and in vivo. Furthermore, we also uncover that TAC-1 and ZYG-9 stabilize each other in C. elegans embryos. CONCLUSIONS: Our findings identify TAC-1 as a core structural and functional member of the evolutionarily conserved TACC family of proteins and suggest that mutual stabilization between TACC and XMAP215 proteins is a key feature ensuring microtubule assembly in vivo.
000089334 6531_ $$aAnimals
000089334 6531_ $$aBlotting
000089334 6531_ $$aWestern
000089334 6531_ $$aCaenorhabditis elegans/*embryology/metabolism
000089334 6531_ $$aChromosome Mapping
000089334 6531_ $$aComparative Study
000089334 6531_ $$aFluorescence Recovery After Photobleaching
000089334 6531_ $$aFluorescent Antibody Technique
000089334 6531_ $$aMicroscopy
000089334 6531_ $$aConfocal
000089334 6531_ $$aMicrotubule-Associated Proteins/*metabolism
000089334 6531_ $$aMicrotubules/*metabolism
000089334 6531_ $$aMitotic Spindle Apparatus/*metabolism
000089334 6531_ $$aPrecipitin Tests
000089334 6531_ $$aRNA Interference
000089334 6531_ $$aResearch Support
000089334 6531_ $$aNon-U.S. Gov't
000089334 700__ $$aBellanger, J. M.
000089334 700__ $$0243625$$aGönczy, P.$$g168676
000089334 773__ $$j13$$k17$$q1488-98$$tCurr Biol
000089334 8564_ $$uhttp://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=12956950$$zURL
000089334 909C0 $$0252248$$pUPGON$$xU11155
000089334 909CO $$ooai:infoscience.tind.io:89334$$pSV$$particle$$qGLOBAL_SET
000089334 937__ $$aUPGON-ARTICLE-2003-001
000089334 970__ $$a12/UPGON
000089334 973__ $$aEPFL$$rREVIEWED$$sPUBLISHED
000089334 980__ $$aARTICLE