The Cysteine-rich Protein Family of Highly Related LIM Domain Proteins

Ralf Weiskirchen(Universität Innsbruck), Josephine D. Pino(University of Utah), Teresita Macalma(University of Utah), Klaus Bister(Universität Innsbruck), Mary C. Beckerle(University of Utah)
Journal of Biological Chemistry
December 1, 1995
Cited by 125Open Access
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Abstract

Here we describe a family of closely related LIM domain proteins in avian cells. The LIM motif defines a zinc-binding domain that is found in a variety of transcriptional regulators, proto-oncogene products, and proteins associated with sites of cell-substratum contact. One type of LIM-domain protein, called the cysteine-rich protein (CRP), is characterized by the presence of two LIM domains linked to short glycine-rich repeats and a potential nuclear localization signal. We have identified and characterized two evolutionarily conserved members of the CRP family, CRP1 and CRP2, in chicken and quail. Expression of the genes encoding both CRP1 and CRP2 is differentially regulated in normal versus transformed cells, raising the possibility that members of the CRP family may function in control of cell growth and differentiation.


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