Accumulation of cytoplasmic dynein and dynactin at microtubule plus ends in Aspergillus nidulans is kinesin dependent. Export

@article{ZhangJ_DyneinDynactinMTplusEndAccumulByKinesin_MBC_2003, abstract = {The mechanism(s) by which microtubule plus-end tracking proteins are targeted is unknown. In the filamentous fungus Aspergillus nidulans, both cytoplasmic dynein and NUDF, the homolog of the LIS1 protein, localize to microtubule plus ends as comet-like structures. Herein, we show that NUDM, the p150 subunit of dynactin, also forms dynamic comet-like structures at microtubule plus ends. By examining proteins tagged with green fluorescent protein in different loss-of-function mutants, we demonstrate that dynactin and cytoplasmic dynein require each other for microtubule plus-end accumulation, and the presence of cytoplasmic dynein is also important for NUDF's plus-end accumulation. Interestingly, deletion of NUDF increases the overall accumulation of dynein and dynactin at plus ends, suggesting that NUDF may facilitate minus-end-directed dynein movement. Finally, we demonstrate that a conventional kinesin, KINA, is required for the microtubule plus-end accumulation of cytoplasmic dynein and dynactin, but not of NUDF.}, author = {Zhang, J. and Li, S. and Fischer, R. and Xiang, X.}, citeulike-article-id = {3836440}, citeulike-linkout-0 = {http://dx.doi.org/10.1091/mbc.E02-08-0516}, citeulike-linkout-1 = {http://view.ncbi.nlm.nih.gov/pubmed/12686603}, citeulike-linkout-2 = {http://www.hubmed.org/display.cgi?uids=12686603}, doi = {10.1091/mbc.E02-08-0516}, issn = {1059-1524}, journal = {Molecular biology of the cell}, keywords = {aspergillus, dynactin, dynein, kinesin, microtubules}, month = {April}, number = {4}, pages = {1479--1488}, posted-at = {2008-12-30 13:29:28}, priority = {0}, title = {Accumulation of cytoplasmic dynein and dynactin at microtubule plus ends in Aspergillus nidulans is kinesin dependent.}, url = {http://dx.doi.org/10.1091/mbc.E02-08-0516}, volume = {14}, year = {2003} }

TY - JOUR ID - ZhangJ_DyneinDynactinMTplusEndAccumulByKinesin_MBC_2003 L3 - citeulike-article-id:3836440 N2 - The mechanism(s) by which microtubule plus-end tracking proteins are targeted is unknown. In the filamentous fungus Aspergillus nidulans, both cytoplasmic dynein and NUDF, the homolog of the LIS1 protein, localize to microtubule plus ends as comet-like structures. Herein, we show that NUDM, the p150 subunit of dynactin, also forms dynamic comet-like structures at microtubule plus ends. By examining proteins tagged with green fluorescent protein in different loss-of-function mutants, we demonstrate that dynactin and cytoplasmic dynein require each other for microtubule plus-end accumulation, and the presence of cytoplasmic dynein is also important for NUDF's plus-end accumulation. Interestingly, deletion of NUDF increases the overall accumulation of dynein and dynactin at plus ends, suggesting that NUDF may facilitate minus-end-directed dynein movement. Finally, we demonstrate that a conventional kinesin, KINA, is required for the microtubule plus-end accumulation of cytoplasmic dynein and dynactin, but not of NUDF. IS - 4 JF - Molecular biology of the cell SN - 1059-1524 EP - 1488 TI - Accumulation of cytoplasmic dynein and dynactin at microtubule plus ends in Aspergillus nidulans is kinesin dependent. VL - 14 SP - 1479 KW - aspergillus KW - dynactin KW - dynein KW - kinesin KW - microtubules AU - Zhang, J AU - Li, S AU - Fischer, R AU - Xiang, X PY - 2003/04// UR - http://dx.doi.org/10.1091/mbc.E02-08-0516 ER -