Regulation of Prelamin a Endoprotease Activity by Prelamin A
Document Type
Article
Publication Date
9-1-1997
Description
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.
Citation Information
Kilic, Fusun; Salas-Marco, Joe; Garland, John; and Sinensky, Michael. 1997. Regulation of Prelamin a Endoprotease Activity by Prelamin A. FEBS Letters. Vol.414(1). 65-68. https://doi.org/10.1016/S0014-5793(97)00989-7 PMID: 9305733 ISSN: 0014-5793