title: Ubiquitination of the human immunodeficiency virus type 1 env glycoprotein.
abstract: Expression of the human immunodeficiency virus type 1 (HIV-1) Env glycoprotein is stringently regulated in infected cells. The majority of the glycoprotein does not reach the cell surface but rather is retained in the endoplasmic reticulum or a cis-Golgi compartment and subsequently degraded. We here report that Env of various HIV-1 isolates is ubiquitinated at the extracellular domain of gp41 and that Env expression could be increased by lactacystin, a specific proteasome inhibitor, suggesting that the ubiquitin/proteasome system is involved in control of expression and degradation.
authors.affiliation: Max-von-Pettenkofer Institut, Genzentrum, LMU München, 81377 Munich, Germany.
authors.forename: A
authors.initials: A
authors.lastname: Bültmann
authors.forename: J
authors.initials: J
authors.lastname: Eberle
authors.forename: J
authors.initials: J
authors.lastname: Haas
mesh_terms: D015700:HIV Envelope Protein gp41 / Q000378:metabolism*; D015497:HIV-1 / Q000378:metabolism*; D006801:Humans; D014452:Ubiquitins / Q000378:metabolism*
chemical_list: D015700:HIV Envelope Protein gp41; D014452:Ubiquitins