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Proteolytic activity associated with the nuclear scaffold. The effect of self-digestion on lamins
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 cy...
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Published in: | The Journal of biological chemistry 1989-09, Vol.264 (25), p.15059-15065 |
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Main Authors: | , |
Format: | Article |
Language: | English |
Subjects: | |
Online Access: | Get full text |
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Summary: | 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. |
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ISSN: | 0021-9258 1083-351X |