Coiled- Coil-Forming Protein Domains
Proc. Natl. Acad. Sci. USA Vol. 92, pp. 3100-3104, April 1995 Biochemistry Stathmin interaction with a putative kinase and coiled-coil-forming protein domains (two-hybrid/regulatory cascades/BiP) ALEXANDRE MAUCUER*t, JACQUES H. CAMONISt, AND ANDRE' SOBEL* *Institut National de la Sante et de la Recherche Medicale, Unit6 153, 17 rue du Fer a Moulin, 75005 Paris, France; and tInstitut National de la Sante et de la Recherche Medicale, Unite 248, 10 Av. de Verdun, 75010 Paris, France Communicated by George A. Olah, University of Southern California, Los Angeles, CA, December 27, 1994 (received for review October 17, 1994) ABSTRACT Stathmin is a ubiquitous, cytosolic 19-kDa in all tissues, the highest level being in brain, where it is mostly protein, which is phosphorylated on up to four sites in present in neurons (21, 22), in testis (18), and in activated or response to many regulatory signals within cells. Its molecular leukemic lymphocytes (5, 23). On the basis of its overall characterization indicates a functional organization including regulatory and molecular features, we proposed that stathmin an N-terminal regulatory domain that bears the phosphory- could act as a general integrator and relay of signals controlling lation sites, linked to a putative a-helical binding domain cell proliferation, differentiation, and functions, during devel- predicted to participate in coiled-coil, protein-protein inter- opment and adult life (2, 24). actions. We therefore proposed that stathmin may play the Phosphorylation studies (25-27), sequence analysis (28-31), role of a relay integrating diverse intracellular regulatory interspecies comparisons (31), and circular dichroism (32) pathways; its action on various target proteins would be a indicate that stathmin is composed of (i) an N-terminal function of its combined phosphorylation state.
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