title: Studies on compartmentation and turnover of murine retrovirus envelope proteins.
abstract: Several aspects of turnover and degradation of cell membrane proteins were studied in an NIH 3T3 cell clone expressing the env gene of Moloney murine leukemia virus ts1. Both internalization and shedding of the extracellular domain of the envelope protein gp70 occurred at the cell surface, albeit, in the case of shedding, only a very small fraction of gp70 was shed. The turnover rate of gp70 at the cell surface was similar to that of the same protein in the postendoplasmic reticulum intracellular compartment. In the presence of L-methionine methyl ester, the transmembrane domain of the envelope protein Prp15E was degraded faster than gp70.
authors.affiliation: University of Texas M. D. Anderson Cancer Center, Science Park-Research Division, Smithville 78957.
authors.forename: Y
authors.initials: Y
authors.lastname: Yu
authors.forename: P K
authors.initials: PK
authors.lastname: Wong
mesh_terms: D016475:3T3 Cells; D000818:Animals; D001692:Biological Transport; D002451:Cell Compartmentation; D002462:Cell Membrane / Q000378:metabolism; D004705:Endocytosis; D004721:Endoplasmic Reticulum / Q000378:metabolism; D015686:Gene Products, env / Q000378:metabolism*; D006056:Golgi Apparatus / Q000378:metabolism; D007425:Intracellular Membranes / Q000378:metabolism; D008562:Membrane Glycoproteins / Q000378:metabolism*; D008715:Methionine / Q000031:analogs & derivatives / Q000494:pharmacology; D051379:Mice; D008979:Moloney murine leukemia virus / Q000378:metabolism*; D011498:Protein Precursors / Q000378:metabolism; D011499:Protein Processing, Post-Translational; D012995:Solubility; D014162:Transfection
chemical_list: D015686:Gene Products, env; D008562:Membrane Glycoproteins; D011498:Protein Precursors; D008715:Methionine; C038344:methionine methyl ester