Ca(2+)-regulated serine protease associated with the nuclear scaffold.

Journal Article

The nuclear scaffold (NS) is a proteinaceous network of orthogonally arrayed intermediate filament proteins, termed lamins, which is responsible for nuclear structure. Recent work has demonstrated that a subset of lamins A/C is proteolytically cleaved to produce an ATP-binding protein. This proteolytic cleavage is accomplished by a NS protease activity, which shows a considerable selectivity for lamins A/C and is stringently regulated by Ca2+ in vitro, suggesting that it might also participate in control of NS breakdown in various scenarios. Here, we identify the major NS protease as a novel serine protease with a predominantly chymotryptic-like substrate preference, and we show that even transient perturbations in cytosolic Ca2+ have significant effects on the NS protease activity. This NS protease activity shows extensive similarities to the multicatalytic proteinase complex. In addition to a potential role in control of NS breakdown at mitosis and/or under pathological conditions, this NS protease is also strategically located for other functions, such as inactivation of various oncogenic proteins or maturation-promoting factor.

Duke Authors

Cited Authors

  • Clawson, GA; Norbeck, LL; Hatem, CL; Rhodes, C; Amiri, P; McKerrow, JH; Patierno, SR; Fiskum, G

Published Date

  • November 1992

Published In

Volume / Issue

  • 3 / 11

Start / End Page

  • 827 - 838

PubMed ID

  • 1467310

International Standard Serial Number (ISSN)

  • 1044-9523

Language

  • eng