CLIP-170 homologue and NUDE play overlapping roles in NUDF localization in Aspergillus nidulans

被引:45
作者
Efimov, VP
Zhang, J
Xiang, X [1 ]
机构
[1] Uniformed Serv Univ Hlth Sci, Dept Biochem & Mol Biol, Bethesda, MD 20814 USA
[2] Univ Med & Dent New Jersey, Robert Wood Johnson Med Sch, Dept Pharmacol, Piscataway, NJ 08854 USA
关键词
D O I
10.1091/mbc.E05-11-1084
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
Proteins in the cytoplasmic dynein pathway accumulate at the microtubule plus end, giving the appearance of comets when observed in live cells. The targeting mechanism for NUDF (LIS1/Pac1) of Aspergillus nidulans, a key component of the dynein pathway, has not been clear. Previous studies have demonstrated physical interactions of NUDF/LIS1/Pac1 with both NUDE/NUDEL/NdI1 and CLIP-170/Bik1. Here, we have identified the A. nidulans CLIP-170 homologue, CLIPA. The clipA deletion did not cause an obvious nuclear distribution phenotype but affected cytoplasmic microtubules in an unexpected manner. Although more microtubules failed to undergo long-range growth toward the hyphal tip at 32 degrees C, those that reached the hyphal tip were less likely to undergo catastrophe. Thus, in addition to acting as a growth-promoting factor, CLIPA also promotes microtubule dynamics. In the absence of CLIPA, green fluorescent protein-labeled cytoplasmic dynein heavy chain, p150(Glued) dynactin, and NUDF were all seen as plus-end comets at 32 degrees C. However, under the same conditions, deletion of both clipA and nudE almost completely abolished NUDF comets, although nudE deletion itself did not cause a dramatic change in NUDF localization. Based on these results, we suggest that CLIPA and NUDE both recruit NUDF to the microtubule plus end. The plus-end localization of CLIPA itself seems to be regulated by different mechanisms under different physiological conditions. Although the KipA kinesin (Kip2/Tea2 homologue) did not affect plus-end localization of CLIPA at 32 degrees C, it was required for enhancing plus-end accumulation of CLIPA at an elevated temperature (42 degrees C).
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页码:2021 / 2034
页数:14
相关论文
共 109 条
[1]  
Akhmanova A, 2005, GENE DEV, V19, P2501, DOI 10.1101/gad.344505
[2]   Microtubule plus-end-tracking proteins: mechanisms and functions [J].
Akhmanova, A ;
Hoogenraad, CC .
CURRENT OPINION IN CELL BIOLOGY, 2005, 17 (01) :47-54
[3]   CLIP-170/tubulin-curved oligomers coassemble at microtubule ends and promote rescues [J].
Arnal, I ;
Heichette, C ;
Diamantopoulos, GS ;
Chrétien, D .
CURRENT BIOLOGY, 2004, 14 (23) :2086-2095
[4]   BIK1, A PROTEIN REQUIRED FOR MICROTUBULE FUNCTION DURING MATING AND MITOSIS IN SACCHAROMYCES-CEREVISIAE, COLOCALIZES WITH TUBULIN [J].
BERLIN, V ;
STYLES, CA ;
FINK, GR .
JOURNAL OF CELL BIOLOGY, 1990, 111 (06) :2573-2586
[5]   Chromosome segregation: Seeing is believing [J].
Bloom, K .
CURRENT BIOLOGY, 2005, 15 (13) :R500-R503
[6]   CLIP170-like tip1p spatially organizes microtubular dynamics in fission yeast [J].
Brunner, D ;
Nurse, P .
CELL, 2000, 102 (05) :695-704
[7]   Tea2p kinesin is involved in spatial microtubule organization by transporting Tip1p on microtubules [J].
Busch, KE ;
Hayles, J ;
Nurse, P ;
Brunner, D .
DEVELOPMENTAL CELL, 2004, 6 (06) :831-843
[8]   Microtubules orient the mitotic spindle in yeast through dynein-dependent interactions with the cell cortex [J].
Carminati, JL ;
Stearns, T .
JOURNAL OF CELL BIOLOGY, 1997, 138 (03) :629-641
[9]   Cell cycle control of kinesin-mediated transport of Bik1 (CLIP-170) regulates microtubule stability and dynein activation [J].
Carvalho, P ;
Gupta, ML ;
Hoyt, MA ;
Pellman, D .
DEVELOPMENTAL CELL, 2004, 6 (06) :815-829
[10]   Surfing on microtubule ends [J].
Carvalho, P ;
Tirnauer, JS ;
Pellman, D .
TRENDS IN CELL BIOLOGY, 2003, 13 (05) :229-237