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Vol. 11, Issue 12, 4159-4171, December 2000

Self-association of Coilin Reveals a Common Theme in Nuclear Body Localization

Michael D. Hebert, and A. Gregory Matera*

Department of Genetics, Center for Human Genetics and Program in Cell Biology, Case Western Reserve University and University Hospitals of Cleveland, Cleveland, Ohio 44106-4955

We have found that coilin, the marker protein for Cajal bodies (coiled bodies, CBs), is a self-interacting protein, and we have mapped the domain responsible for this activity to the amino-terminus. Together with a nuclear localization signal, the self-interaction domain is necessary and sufficient for localization to CBs. Overexpression of various wild-type and mutant coilin constructs in HeLa cells results in disruption of both CBs and survival motor neurons (SMN) gems. Additionally, we have identified a cryptic nucleolar localization signal (NoLS), within the coilin protein, which may be exposed in specific coilin phospho-isoforms. The implications of these findings are discussed in light of the fact that other proteins known to localize within nuclear bodies (e.g., PML, SMN and Sam68) can also self-associate. Thus protein self-interaction appears to be a general feature of nuclear body marker proteins.

* Corresponding editor. E-mail address: gxm26{at}po.cwru.edu

Molecular Biology of the Cell
Vol. 11, 4159-4171, December 2000
Copyright © 2000 by The American Society for Cell Biology


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