Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1991-3-8
pubmed:abstractText
Sorting of prohormones and propeptides into secretory vesicles at the trans-Golgi face probably depends on a signal contained within the amino acid sequence of the peptide. To date no consensus sequence has been identified in prohormones or propeptides that might serve such a targeting function. In this report, we have analyzed the amino acid sequences and secondary structures of 15 prohormones and propeptides that have been shown experimentally to be sorted to secretory vesicles when the corresponding cDNA is transfected into mouse pituitary AtT20 cells. From these analyses, we have identified a motif that is shared by all of these diverse propeptides and might serve as a vesicular targeting sequence. This motif is degenerate and consists of two or more leucines occupying one side of a highly amphipattic alpha helix with a serine (or rarely threonine) positioned N-terminal to the leucines and projecting to the same side of the helix.
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:issnType
Print
pubmed:day
31
pubmed:volume
174
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
586-92
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1991
pubmed:articleTitle
A motif found in propeptides and prohormones that may target them to secretory vesicles.
pubmed:affiliation
Department of Medicine, University of North Carolina, Chapel Hill 27599-7250.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't