Publication Date:
2001-06-02
Description:
The GGAs are a multidomain protein family implicated in protein trafficking between the Golgi and endosomes. Here, the VHS domain of GGA2 was shown to bind to the acidic cluster-dileucine motif in the cytoplasmic tail of the cation-independent mannose 6-phosphate receptor (CI-MPR). Receptors with mutations in this motif were defective in lysosomal enzyme sorting. The hinge domain of GGA2 bound clathrin, suggesting that GGA2 could be a link between cargo molecules and clathrin-coated vesicle assembly. Thus, GGA2 binding to the CI-MPR is important for lysosomal enzyme targeting.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhu, Y -- Doray, B -- Poussu, A -- Lehto, V P -- Kornfeld, S -- R01 CA-08759/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2001 Jun 1;292(5522):1716-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Internal Medicine, Washington University School of Medicine, 660 South Euclid Avenue, St. Louis, MO 63110, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11387476" target="_blank"〉PubMed〈/a〉
Keywords:
Adaptor Proteins, Vesicular Transport
;
Amino Acid Motifs
;
Amino Acid Sequence
;
Animals
;
*Carrier Proteins
;
Cations
;
Clathrin/metabolism
;
Dipeptides/chemistry/metabolism
;
L Cells (Cell Line)
;
Lysosomes/*enzymology
;
Mice
;
Molecular Sequence Data
;
Mutation
;
Protein Sorting Signals
;
Protein Structure, Tertiary
;
*Protein Transport
;
Proteins/chemistry/genetics/*metabolism
;
Rats
;
Receptor, IGF Type 2/*chemistry/genetics/*metabolism
;
Recombinant Fusion Proteins/chemistry/metabolism
;
Solubility
;
Transcription Factor AP-1/metabolism
;
Transport Vesicles/metabolism
;
Two-Hybrid System Techniques
;
trans-Golgi Network/metabolism
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
