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

Authors
  • Clawson, G A
  • Norbeck, L L
  • Hatem, C L
  • Rhodes, C
  • Amiri, P
  • McKerrow, J H
  • Patierno, S R
  • Fiskum, G
Type
Published Article
Journal
Cell growth & differentiation : the molecular biology journal of the American Association for Cancer Research
Publisher
Philadelphia, PA : The Association
Publication Date
Nov 01, 1992
Volume
3
Issue
11
Pages
827–838
Identifiers
PMID: 1467310
Source
Medline
License
Unknown

Abstract

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.

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