Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1993-2-18
pubmed:abstractText
We have investigated the mechanism by which LAMP-1, a principal protein of the lysosomal membrane, is targeted to lysosomes. Mutagenesis and transfection experiments indicate that the motif Tyr-X-X-hydrophobic residue at the carboxyl terminus of the 11-amino acid cytoplasmic tail of the protein constitutes the lysosomal targeting signal for LAMP-1. This motif directs CD44, a cell surface hyaluronate receptor, to the lysosomal membrane, but only when the signal is placed at the carboxyl-terminus of a truncated cytoplasmic tail. The signal did not confer lysosomal targeting when it was situated internally or at the carboxyl terminus of the normal CD44 cytoplasmic tail. An apparent paradox is that similar Tyr-containing sequences mediate internalization, but not lysosomal targeting, of several receptors. Of possible relevance is the additional finding that purified LAMP-1 protein lacks the two carboxyl-terminal residues predicted by cDNA, both of which are essential for proper trafficking. A model is proposed in which lysosomal targeting is distinguished from receptor internalization through proteolytic modification of the internalization signal.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
268
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1941-6
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:8420968-Amino Acid Sequence, pubmed-meshheading:8420968-Animals, pubmed-meshheading:8420968-Antigens, CD, pubmed-meshheading:8420968-Base Sequence, pubmed-meshheading:8420968-Cell Line, pubmed-meshheading:8420968-Cytoplasm, pubmed-meshheading:8420968-DNA, pubmed-meshheading:8420968-Humans, pubmed-meshheading:8420968-Intracellular Membranes, pubmed-meshheading:8420968-Lysosome-Associated Membrane Glycoproteins, pubmed-meshheading:8420968-Lysosomes, pubmed-meshheading:8420968-Membrane Glycoproteins, pubmed-meshheading:8420968-Mice, pubmed-meshheading:8420968-Molecular Sequence Data, pubmed-meshheading:8420968-Mutagenesis, Site-Directed, pubmed-meshheading:8420968-Peptide Fragments, pubmed-meshheading:8420968-Protein Sorting Signals, pubmed-meshheading:8420968-Receptors, Lymphocyte Homing, pubmed-meshheading:8420968-Transfection, pubmed-meshheading:8420968-Trypsin
pubmed:year
1993
pubmed:articleTitle
The motif Tyr-X-X-hydrophobic residue mediates lysosomal membrane targeting of lysosome-associated membrane protein 1.
pubmed:affiliation
Department of Pharmacology and Molecular Sciences, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't