Linked Life Data

9920732

Source:http://linkedlifedata.com/resource/pubmed/id/9920732

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1999-2-25
pubmed:abstractText
The Shaker superfamily encodes voltage-gated potassium (Kv) channels. The amino (N) terminus is important for channel assembly and mediates fast inactivation. We recently isolated a Kv channel from rabbit kidney, denoted rabKv1.3 (Yao et al., J. Clin. Invest. 97, 2525-2533, 1996) and found that deleting a region (T0 domain, amino acids 3-39) proximal to the T1 recognition domain (a.a 42-185) leads to a 13-fold amplification of Kv current as compared to wild type channels (Yao et al., BBRC 249, 492-498). Here we show that deleting the T0 domain affects neither single channel conductance nor channel open probability. Instead, it increases the absolute number of channel proteins present in the membrane. We conclude that the T0 domain is a previously unrecognized Shaker Kv1.3, N-terminal regulatory region that modulates steady state channel protein density in the plasma membrane.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0006-291X
pubmed:author
pubmed:copyrightInfo
Copyright 1999 Academic Press.
pubmed:issnType
Print
pubmed:day
8
pubmed:volume
254
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
54-64
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1999
pubmed:articleTitle
The T0 domain of rabbit KV1.3 regulates steady state channel protein level.
pubmed:affiliation
Department of Medicine, University of Vermont, Burlington, Vermont, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't