Linked Life Data

8567675

Source:http://linkedlifedata.com/resource/pubmed/id/8567675

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1996-3-1
pubmed:abstractText
The transport of proteins from the secretory to the endocytic pathway is mediated by carrier vesicles coated with the AP-1 Golgi assembly proteins and clathrin. The mannose 6-phosphate receptors (MPHs) are two major transmembrane proteins segregated into these transport vesicles. Together with the GTPase ARF-1, these cargo proteins are essential components for the efficient translocation of the cytosolic AP-1 onto membranes of the trans-Golgi network, the first step of clathrin coat assembly, MPR-negative fibroblasts have a low capacity of recruiting AP-1 which can be restored by re-expressing the MPRs in these cells. This property was used to identify the protein motif of the cation-dependent mannose 6-phosphate receptor (CD-MPR) cytoplasmic domain that is essential for these interactions. Thus, the affinity of AP-1 for membranes and in vivo transport of cathepsin D were measured for MPR-negative cells re-expressing various CD-MPR mutants. The results indicate that the targeting of lysosomal enzymes requires the CD-PDR cytoplasmic domain that are different from tyrosine-based endocytosis motifs. The first is a casein kinase II phosphorylation site (ESEER) that is essential for high affinity binding of AP-1 and therefore probably acts as a dominant determinant controlling CD-MPR sorting in the trans-Golgi network. The second is the adjacent di-leucine motif (HLLPM), which, by itself, is not critical for AP-1 binding, but is absolutely required for a downstream sorting event.
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
26
pubmed:volume
271
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2171-8
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:8567675-Adaptor Proteins, Vesicular Transport, pubmed-meshheading:8567675-Animals, pubmed-meshheading:8567675-Base Sequence, pubmed-meshheading:8567675-Casein Kinase II, pubmed-meshheading:8567675-Cathepsin D, pubmed-meshheading:8567675-Cell Compartmentation, pubmed-meshheading:8567675-Cells, Cultured, pubmed-meshheading:8567675-Coated Vesicles, pubmed-meshheading:8567675-DNA Primers, pubmed-meshheading:8567675-Endocytosis, pubmed-meshheading:8567675-Golgi Apparatus, pubmed-meshheading:8567675-Intracellular Membranes, pubmed-meshheading:8567675-Lysosomes, pubmed-meshheading:8567675-Mice, pubmed-meshheading:8567675-Molecular Sequence Data, pubmed-meshheading:8567675-Mutagenesis, Site-Directed, pubmed-meshheading:8567675-Nerve Tissue Proteins, pubmed-meshheading:8567675-Phosphoproteins, pubmed-meshheading:8567675-Phosphorylation, pubmed-meshheading:8567675-Protein-Serine-Threonine Kinases, pubmed-meshheading:8567675-Receptor, IGF Type 2, pubmed-meshheading:8567675-Structure-Activity Relationship, pubmed-meshheading:8567675-Transfection
pubmed:year
1996
pubmed:articleTitle
A casein kinase II phosphorylation site in the cytoplasmic domain of the cation-dependent mannose 6-phosphate receptor determines the high affinity interaction of the AP-1 Golgi assembly proteins with membranes.
pubmed:affiliation
European Molecular Biology Laboratory, Heidelberg, Federal Republic of Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't