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

Gary Clawson, L. L. Norbeck, C. L. Hatem, C. Rhodes, P. Amiri, J. H. McKerrow, S. R. Patierno, G. Fiskum

Research output: Contribution to journalArticlepeer-review

53 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)827-838
Number of pages12
JournalCell growth & differentiation : the molecular biology journal of the American Association for Cancer Research
Volume3
Issue number11
StatePublished - Nov 1992

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Cell Biology

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