Cooperative ATP binding by cloned lamin C
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Updated: Sep 15, 2026

Aip1p Dynamics Are Altered by the R256H Mutation in Actin
Published on: July 30, 2014
1Department of Pathology, George Washington University, Washington, D.C. 20037.
Abstract:
Cloned human lamin C was expressed in and purified from bacteria and used in ATP binding assays. Scatchard analysis revealed strong positive cooperative and noncooperative binding, with estimated apparent dissociation constants of 3 X 10(-6) and 2 X 10(-5) M, respectively. The binding is strongly pH dependent. ATP binding by lamins A/C (presumably as intermediate filaments) may provide a substantial storage depot for ATP at the peripheral lamina for use by a number of ATP-requiring nuclear scaffold enzymes.
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