Lis1 Has Two Opposing Modes of Regulating Cytoplasmic Dynein
نویسندگان
چکیده
منابع مشابه
Regulation of cytoplasmic dynein ATPase by Lis1.
Mutations in Lis1 cause classical lissencephaly, a developmental brain abnormality characterized by defects in neuronal positioning. Over the last decade, a clear link has been forged between Lis1 and the microtubule motor cytoplasmic dynein. Substantial evidence indicates that Lis1 functions in a highly conserved pathway with dynein to regulate neuronal migration and other motile events. Yeast...
متن کاملRoles of Lissencephaly Gene, LIS1, in Regulating Cytoplasmic Dynein Functions: a Dissertation
Spontaneous mutations in the human LIS 1 gene are responsible for Type I lissencephaly (" smooth brain ). The distribution of neurons within the cerebral cortex of lissencephalic children appears randomized, probably owing to a defect in neuronal migration during early development. LIS 1 has been implicated in the dynein pathway by genetic analyses in fungi. We previously reported that the vert...
متن کاملTwo modes of microtubule sliding driven by cytoplasmic dynein.
Dynein is a huge multisubunit microtubule (MT)-based motor, whose motor domain resides in the heavy chain. The heavy chain comprises a ring of six AAA (ATPases associated with diverse cellular activities) modules with two slender protruding domains, the tail and stalk. It has been proposed that during the ATP hydrolysis cycle, this tail domain swings against the AAA ring as a lever arm to gener...
متن کاملNeurobiology of Disease Regulation of Cytoplasmic Dynein ATPase by Lis1
Mariano T. Mesngon,1 Cataldo Tarricone,3 Sachin Hebbar,1 Aimee M. Guillotte,1 E. William Schmitt,2 Lorene Lanier,4 Andrea Musacchio,3 Stephen J. King,2 and Deanna S. Smith1 1Department of Biological Sciences, University of South Carolina, Columbia, South Carolina 29208, 2Division of Molecular Biology and Biochemistry, University of Missouri–Kansas City, Kansas City, Missouri 64110, 3Department ...
متن کاملDynactin has two antagonistic regulatory domains and exerts opposing effects on dynein motility
Dynactin is a dynein-regulating protein that increases the processivity of dynein movement on microtubules. Recent studies have shown that a tripartite complex of dynein-dynactin-Bicaudal D2 is essential for highly processive movement. To elucidate the regulation of dynein motility by dynactin, we focused on two isoforms (A and B) of dynactin 1 (DCTN1), the largest subunit of dynactin that cont...
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ژورنال
عنوان ژورنال: Cell
سال: 2017
ISSN: 0092-8674
DOI: 10.1016/j.cell.2017.08.037