Literature DB >> 9594664

LIM domains: multiple roles as adapters and functional modifiers in protein interactions.

I B Dawid1, J J Breen, R Toyama.   

Abstract

The LIM domain is a specialized double-zinc finger motif found in a variety of proteins, in association with domains of divergent functions or forming proteins composed primarily of LIM domains. LIM domains interact specifically with other LIM domains and with many different protein domains. LIM domains are thought to function as protein interaction modules, mediating specific contacts between members of functional complexes and modulating the activity of some of the constituent proteins. Nucleic acid binding by LIM domains, while suggested by structural considerations, remains an unproven possibility. LIM-domain proteins can be nuclear, cytoplasmic, or can shuttle between compartments. Several important LIM proteins are associated with the cytoskeleton, having a role in adhesion-plaque and actin-microfilament organization. Among nuclear LIM proteins, the LIM homeodomain proteins form a major subfamily with important functions in cell lineage determination and pattern formation during animal development.

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Year:  1998        PMID: 9594664     DOI: 10.1016/s0168-9525(98)01424-3

Source DB:  PubMed          Journal:  Trends Genet        ISSN: 0168-9525            Impact factor:   11.639


  171 in total

1.  The N-terminal LIM domain negatively regulates the kinase activity of LIM-kinase 1.

Authors:  K Nagata; K Ohashi; N Yang; K Mizuno
Journal:  Biochem J       Date:  1999-10-01       Impact factor: 3.857

2.  The balance between isoforms of the prickle LIM domain protein is critical for planar polarity in Drosophila imaginal discs.

Authors:  D Gubb; C Green; D Huen; D Coulson; G Johnson; D Tree; S Collier; J Roote
Journal:  Genes Dev       Date:  1999-09-01       Impact factor: 11.361

3.  Chip interacts with diverse homeodomain proteins and potentiates bicoid activity in vivo.

Authors:  E Torigoi; I M Bennani-Baiti; C Rosen; K Gonzalez; P Morcillo; M Ptashne; D Dorsett
Journal:  Proc Natl Acad Sci U S A       Date:  2000-03-14       Impact factor: 11.205

4.  LPP, an actin cytoskeleton protein related to zyxin, harbors a nuclear export signal and transcriptional activation capacity.

Authors:  M M Petit; J Fradelizi; R M Golsteyn; T A Ayoubi; B Menichi; D Louvard; W J Van de Ven; E Friederich
Journal:  Mol Biol Cell       Date:  2000-01       Impact factor: 4.138

5.  TRIADs: a new class of proteins with a novel cysteine-rich signature.

Authors:  B A van der Reijden; C A Erpelinck-Verschueren; B Löwenberg; J H Jansen
Journal:  Protein Sci       Date:  1999-07       Impact factor: 6.725

6.  Ajuba, a cytosolic LIM protein, shuttles into the nucleus and affects embryonal cell proliferation and fate decisions.

Authors:  J Kanungo; S J Pratt; H Marie; G D Longmore
Journal:  Mol Biol Cell       Date:  2000-10       Impact factor: 4.138

7.  Fine mapping of the alpha-actinin binding site within cysteine-rich protein.

Authors:  B D Harper; M C Beckerle; P Pomiès
Journal:  Biochem J       Date:  2000-08-15       Impact factor: 3.857

8.  Intraresidue 1H-15N-13C' and 1H alpha-13C alpha-13C' dipole-CSA relaxation interference as a source of constraints for structural refinement of metal-binding sites in zinc-finger proteins.

Authors:  K Kloiber; W Schüler; R Konrat
Journal:  J Biomol NMR       Date:  2001-04       Impact factor: 2.835

9.  Transcriptional activation by the PHD finger is inhibited through an adjacent leucine zipper that binds 14-3-3 proteins.

Authors:  T Halbach; N Scheer; W Werr
Journal:  Nucleic Acids Res       Date:  2000-09-15       Impact factor: 16.971

10.  Ajuba, a novel LIM protein, interacts with Grb2, augments mitogen-activated protein kinase activity in fibroblasts, and promotes meiotic maturation of Xenopus oocytes in a Grb2- and Ras-dependent manner.

Authors:  R K Goyal; P Lin; J Kanungo; A S Payne; A J Muslin; G D Longmore
Journal:  Mol Cell Biol       Date:  1999-06       Impact factor: 4.272

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