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Dynamin-like protein encoded by the Drosophila shibire gene associated with vesicular traffic.

Abstract：

:Temperature-sensitive paralysis is the most striking defect of adult Drosophila carrying the shibire mutation. This is believed to be due to a reversible block of endocytosis, which prevents membrane cycling and thus depletes synaptic vesicles. The shibire mutation also affects many tissues outside the nervous system. We have now mapped and characterized the shibire gene. A 275-kilobase yeast artificial chromosome was subcloned into cosmids, among which the gene was then located by analysing with restriction-fragment length polymorphisms. A 15-kilobase fragment of wild-type DNA rescues the mutant phenotype and the sequence of two mutant alleles show differences with wild type, demonstrating that we have isolated the shibire gene. The gene encodes a protein that is highly similar to rat dynamin, 69% of the amino-acid sequence is identical. Dynamin is a GTP-driven mechanochemical enzyme related to mammalian mx-proteins and to the yeast vps 1 gene product. Because the shibire gene product and dynamin have extensive similarity, we propose that they are cognate homologues. Dynamin causes microtubules to slide along each other in vitro and in extracts it is associated with a distinct, but so far uncharacterized, membrane fraction. In light of the shibire phenotype, we suggest that these proteins provide the motor for vesicular transport during endocytosis.

journal_name

Nature

journal_title

Nature

authors

van der Bliek AM,Meyerowitz EM

doi

10.1038/351411a0

subject

Has Abstract

pub_date

1991-05-30 00:00:00

pages

411-4

issue

6325

eissn

0028-0836

issn

1476-4687

journal_volume

351

pub_type

杂志文章

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