TY - JOUR
T1 - NudEL targets dynein to microtubule ends through LIS1
AU - Li, Jun
AU - Lee, Wei Lih
AU - Cooper, John A.
N1 - Funding Information:
We are grateful to R. Heil-Chapdelaine and S. Nelson for their advice and assistance. This work was supported by the American Heart Association Fellowship AHA40390 to J.L., Damon Runyon Cancer Research Foundation Fellowship DRG -1671 to W.-L.L., and NIH GM47337 to J.A.C.
PY - 2005/7
Y1 - 2005/7
N2 - Dynein is a minus-end-directed microtubule motor with critical roles in mitosis, membrane transport and intracellular transport. Several proteins regulate dynein activity, including dynactin, LIS1 (refs 2, 3) and NudEL (NudE-like). Here, we identify a NUDEL homologue in budding yeast and name it Ndl1. The ndl1Δ null mutant shows decreased targeting of dynein to microtubule plus ends, an essential element of the model for dynein function. We find that Ndl1 regulates dynein targeting through LIS1, with which it interacts biochemically, but not through CLIP170, another plus-end protein involved in dynein targeting. Ndl1 is found at far fewer microtubule ends than are LIS1 and dynein. However, when Ndl1 is present at a plus end, the molar amount of Ndl1 approaches that of LIS1 and dynein. We propose a model in which Ndl1 binds transiently to the plus end to promote targeting of LIS1, which cooperatively recruits dynein.
AB - Dynein is a minus-end-directed microtubule motor with critical roles in mitosis, membrane transport and intracellular transport. Several proteins regulate dynein activity, including dynactin, LIS1 (refs 2, 3) and NudEL (NudE-like). Here, we identify a NUDEL homologue in budding yeast and name it Ndl1. The ndl1Δ null mutant shows decreased targeting of dynein to microtubule plus ends, an essential element of the model for dynein function. We find that Ndl1 regulates dynein targeting through LIS1, with which it interacts biochemically, but not through CLIP170, another plus-end protein involved in dynein targeting. Ndl1 is found at far fewer microtubule ends than are LIS1 and dynein. However, when Ndl1 is present at a plus end, the molar amount of Ndl1 approaches that of LIS1 and dynein. We propose a model in which Ndl1 binds transiently to the plus end to promote targeting of LIS1, which cooperatively recruits dynein.
UR - http://www.scopus.com/inward/record.url?scp=22144491144&partnerID=8YFLogxK
U2 - 10.1038/ncb1273
DO - 10.1038/ncb1273
M3 - Article
C2 - 15965467
AN - SCOPUS:22144491144
SN - 1465-7392
VL - 7
SP - 686
EP - 690
JO - Nature Cell Biology
JF - Nature Cell Biology
IS - 7
ER -