Multiple domains in caveolin-1 control its intracellular traffic

Citation
T. Machleidt et al., Multiple domains in caveolin-1 control its intracellular traffic, J CELL BIOL, 148(1), 2000, pp. 17-28
Citations number
39
Categorie Soggetti
Cell & Developmental Biology
Journal title
JOURNAL OF CELL BIOLOGY
ISSN journal
00219525 → ACNP
Volume
148
Issue
1
Year of publication
2000
Pages
17 - 28
Database
ISI
SICI code
0021-9525(20000110)148:1<17:MDICCI>2.0.ZU;2-4
Abstract
Caveolin-1 is an integral membrane protein of caveolae that is thought to p lay an important role in both the traffic of cholesterol to caveolae and mo dulating the activity of multiple signaling molecules at this site. The mol ecule is synthesized in the endoplasmic reticulum, transported to the cell surface, and undergoes a poorly understood recycling itinerary. We have use d mutagenesis to determine the parts of the molecule that control traffic o f caveolin-1 from its site of synthesis to the cell surface, We identified four regions of the molecule that appear to influence caveolin-1 traffic, A region between amino acids 66 and 70, which is in the most conserved regio n of the molecule, is necessary for exit from the endoplasmic reticulum. Th e region between amino acids 71 and 80 controls incorporation of caveolin-1 oligomers into detergent-resistant regions of the Golgi apparatus. Amino a cids 91-100 and 134-154 both control oligomerization and exit from the Golg i apparatus. Removal of other portions of the molecule has no effect on tar geting of newly synthesized caveolin-1 to caveolae, The results suggest tha t movement of caveolin-1 among various endomembrane compartments is control led at multiple steps.