Linked Life Data

18817524

Source:http://linkedlifedata.com/resource/pubmed/id/18817524

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
11
pubmed:dateCreated
2008-10-20
pubmed:abstractText
Transport of proteins and lipids between intracellular compartments is fundamental to the organization and function of eukaryotic cells. The efficiency of this process is greatly enhanced through coupling of membranes to microtubules. This serves two functions, organelle positioning and vesicular transport. In this study, we show that in addition to the well-known role for the minus-end motor dynein in endoplasmic reticulum (ER)-to-Golgi transport, the plus-end-directed motor kinesin-1 is involved in positioning coat protein II-coated ER exit sites (ERES) in cells as well as the formation of transport carriers and their movement to the Golgi. Using two-dimensional Gaussian fitting to determine their location at high spatial resolution, we show that ERES undergo short-range bidirectional movements. Bidirectionality depends on both kinesin-1 and dynein. Suppression of kinesin-1 (KIF5B) also inhibits ER-to-Golgi transport and affects the morphology of ER-to-Golgi transport carriers. Furthermore, we show that suppression of dynein heavy chain expression increases the range of movement of ERES, suggesting that dynein might anchor ERES, or the ER itself, to microtubules. These data implicate kinesin-1 in the spatial organization of the ER/Golgi interface as well as in traffic outside the ER.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
1600-0854
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
9
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1850-66
pubmed:dateRevised
2009-8-28
pubmed:meshHeading
pubmed:year
2008
pubmed:articleTitle
Kinesin-1 (uKHC/KIF5B) is required for bidirectional motility of ER exit sites and efficient ER-to-Golgi transport.
pubmed:affiliation
Cell Biology Laboratories, Department of Biochemistry, University of Bristol, School of Medical Sciences, University Walk, Bristol, BS81TD, UK.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't