Regulation of prelamin A endoprotease activity by prelamin A

FEBS Letters

Salas-Marco, Joe¹  Garland, John¹  Kilic, Fusun¹  Sinensky, Michael¹ 

[1] Department of Biochemistry and Molecular Biology, James H. Quillen College of Medicine, East Tennessee State University, Box 70581, Johnson City, TN 37614-0581, USA

关键词: Prelamin A endoprotease;    Prelamin A;    HeLa cell;    Promyelocytic leukemia cell (HL60);    Teratocarcinoma cell (F9);   

DOI  :  10.1016/S0014-5793(97)00989-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The maturation of lamin A is completed by the endoproteolytic cleavage of its farnesylated precursor protein, prelamin A. In the absence of this cleavage, prelamin A can neither give rise to lamin A nor assemble into the nuclear lamina. We call the enzyme which catalyzes this endoproteolytic step the `prelamin A endoprotease'. In this study, we begin characterization of the regulation of prelamin A endoprotease. In particular, we address the question as to whether prelamin A endoprotease activity is constitutive in cells or responds to expression of prelamin A. To do this, we compared the activity of this novel endoprotease in cells which express prelamin A with those that do not. Our data shows that the enzymatic activity of prelamin A endoprotease is enhanced by the expression of prelamin A.

【 授权许可】

Unknown