Proteolytic activity associated with the nuclear scaffold. The effect of self-digestion on lamins

Z. A. Tokes, G. A. Clawson

Research output: Contribution to journalArticle

40 Scopus citations

Abstract

The inner aspect of the nuclear envelope is supported by a peripheral framework called the nuclear scaffold, which consists of both structural and functional proteins. Its major structural components, lamins A-C, form a highly polymerized and insoluble fibrous matrix during interphase of the cell cycle. Functional constituents of the scaffold include the 46-kDa nucleoside triphosphatase which is thought to participate in nucleocytoplasmic transport of mRNA. This 46-kDa component shares an amino-terminal sequence with lamins A and C, indicating that proteolytic remodeling of the nuclear scaffold may contribute to the generation of nucleoside triphosphatase activity (Clawson, G.A., Lackey, A., and Tokes, Z.A. (1988) Exp. Cell Res. 176, 180-186). We report here that neutral protease activity intimately associated with the nuclear scaffold is also a functional constituent. This activity has a considerable selectivity for lamins as shown by self-digestion of scaffold preparations, and it may participate in the remodeling of the nuclear scaffold after treatment with carcinogens.

Original languageEnglish (US)
Pages (from-to)15059-15065
Number of pages7
JournalJournal of Biological Chemistry
Volume264
Issue number25
StatePublished - Jan 1 1989

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Fingerprint Dive into the research topics of 'Proteolytic activity associated with the nuclear scaffold. The effect of self-digestion on lamins'. Together they form a unique fingerprint.

  • Cite this