Work

Proteolytic Activity Associated with the Nuclear Scaffold

Year: 1989

Type: article

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 Tökés, 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.

Source: Journal of Biological Chemistry

DOI: 10.1016/s0021-9258(18)63810-4

Authors: Z A Tökés, G A Clawson

Institution: University of Southern California

Language: English

Topic: Nuclear Structure and Function

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: hybrid

Estimated APC paid: $3,430

Funder: National Cancer Institute