title: The CRP/MLP/TLP family of LIM domain proteins: acting by connecting.
abstract: In vertebrates, members of the cysteine-rich protein (CRP) family are characterized by the presence of two LIM domains linked to short glycine-rich repeats. These proteins mediate protein-protein interactions and are of fundamental importance for cell differentiation, cytoskeletal remodeling, and transcriptional regulation. To date, a vast amount of information about vertebrate CRPs has become available, including their biological functions, interacting partners, and three-dimensional structures. Compatible with a molecular adapter role, structural data reveal that the LIM domains within these proteins represent completely independent folded units bridged by flexible linker regions. The physiological roles for individual CRPs was determined by targeted gene disruption analysis and by identification of common and specific binding partners by means of yeast and mammalian two-hybrid screens. Several CRP-like LIM domain proteins with close structural and sequence similarity were identified in arthropods, protozoas and plants, supporting the notion that this subset of LIM domain proteins has been highly conserved over the span of evolution thereby emphasizing the importance of their function.
authors.affiliation: Institute of Clinical Chemistry and Pathobiochemistry, RWTH- University Hospital, D-52074 Aachen, Germany. rweiskirchen@ukaachen.de
authors.forename: Ralf
authors.initials: R
authors.lastname: Weiskirchen
authors.forename: Kalle
authors.initials: K
authors.lastname: Günther
mesh_terms: D048868:Adaptor Proteins, Signal Transducing; D000595:Amino Acid Sequence; D000818:Animals; D052004:Bone Morphogenetic Protein Receptors; D015870:Gene Expression; D018390:Gene Targeting; D006801:Humans; D060588:LIM Domain Proteins; D008565:Membrane Proteins; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009687:Nuclear Proteins / Q000737:chemistry / Q000235:genetics / Q000502:physiology; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry* / Q000235:genetics / Q000502:physiology*; D017386:Sequence Homology, Amino Acid
chemical_list: D048868:Adaptor Proteins, Signal Transducing; C486175:CRIM1 protein, human; C486176:CRIP2 protein, human; D060588:LIM Domain Proteins; D008565:Membrane Proteins; D009687:Nuclear Proteins; D011506:Proteins; C074370:cysteine-rich protein, mammalian; D052004:Bone Morphogenetic Protein Receptors