Degradation of stearoyl-coenzyme A desaturase: endoproteolytic cleavage by an integral membrane protease.

Abstract:

:Stearoyl-coenzyme A desaturase (SCD) is a key regulator of membrane fluidity, turns over rapidly, and represents a prototype for selective degradation of resident proteins of the endoplasmic reticulum. Using detergent-solubilized, desaturase-induced rat liver microsomes we have characterized a protease that degrades SCD. Degradation of SCD in vitro is highly selective, has a half-life of 3-4 h, and generates a 20-kDa C-terminal fragment of SCD. The N terminus of the 20-kDa fragment was identified as Phe177. The cleavage site occurs in a conserved 12-residue hydrophobic segment of SCD flanked by clusters of basic residues. The SCD protease remains associated with microsomal membranes after peripheral and lumenal proteins have been selectively removed. SCD protease is present in normal rat liver microsomes and cleaves purified SCD. We conclude that rapid turnover of SCD involves a constitutive microsomal protease with properties of an integral membrane protein.

journal_name

Mol Biol Cell

authors

Heinemann FS,Ozols J

doi

10.1091/mbc.9.12.3445

subject

Has Abstract

pub_date

1998-12-01 00:00:00

pages

3445-53

issue

12

eissn

1059-1524

issn

1939-4586

journal_volume

9

pub_type

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