Linked Life Data

2475643

Source:http://linkedlifedata.com/resource/pubmed/id/2475643

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1989-10-3
pubmed:abstractText
Clathrin plays an important role in many cellular processes, including endocytosis, secretion, and sorting of membranous organelles. Both the neuronal cell body and presynaptic terminals contain numerous coated vesicles, but few are detectable in the axonal regions that connect these two regions of the neuron. Clathrin heavy chains, light chains, and assembly proteins have all been shown to be axonally transported as part of slow component b (SCb). However, the paucity of coated vesicles present in the axon indicates the existence of a mechanism regulating clathrin coated assembly in vivo. A clathrin uncoating ATPase has been described that binds in stoichiometric amounts to clathrin and dissociates clathrin coats from vesicles in the presence of ATP in vitro. This clathrin uncoating ATPase is a major cytosolic protein of Mr 70 kD in bovine brain, forming 1% of soluble brain protein, and appears to be homologous with a constitutively expressed 70 kd heat shock protein (HSC70). We report here that a major 70 kD protein present in the SCb rate component of axonal transport is identical with HSC70 by both biochemical and immunochemical criteria. The cotransport of HSC70 with clathrin in SCb of axonal transport is consistent with a role for HSC70 in vivo in the regulation of clathrin function during axonal transport.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0360-4012
pubmed:author
pubmed:issnType
Print
pubmed:volume
23
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
433-40
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
Axonal transport of a clathrin uncoating ATPase (HSC70): a role for HSC70 in the modulation of coated vesicle assembly in vivo.
pubmed:affiliation
Department of Cell Biology, University of Texas Southwestern Medical Center, Dallas 75235.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't