title: PINCH2 is a new five LIM domain protein, homologous to PINCHand localized to focal adhesions.
abstract: PINCH is a five LIM domain protein involved in the regulation of integrin-mediated cell adhesion. It has been shown that PINCH interacts with integrin-linked kinase and Nck2. Here we describe a new isoform of PINCH, which we call PINCH2. Therefore, we rename PINCH to PINCH1. PINCH2 has an overall similarity of 92% to PINCH1 and contains five LIM domains like PINCH1. While protein and gene structure of the PINCH homologues are very similar and well conserved during evolution, we observed differential expression pattern of the mRNAs. Based on northern hybridization of mouse embryo RNA, PINCH1 is already detectable at E8.5. It is highly expressed during later stages of development and in all adult mouse tissues analyzed, with the highest levels in heart, lung, bladder, skin, and uterus. In contrast, significant PINCH2 expression starts at E14.5. In adult mice it is widely expressed, similar to PINCH1, but absent from spleen and thymus. In situ hybridization confirmed the Northern data and showed differential expression of PINCH1 and PINCH2 in embryonic intestine. Finally, we demonstrate that PINCH2 localizes to focal adhesions in NIH 3T3 cells and to Z-disks in primary rat cardiomyocytes.
authors.affiliation: Max Planck Institute for Biochemistry, Department of Molecular Medicine, Martinsried, Germany.
authors.forename: Attila
authors.initials: A
authors.lastname: Braun
authors.forename: Randi
authors.initials: R
authors.lastname: Bordoy
authors.forename: Fabio
authors.initials: F
authors.lastname: Stanchi
authors.forename: Markus
authors.initials: M
authors.lastname: Moser
authors.forename: Günter
authors.initials: G
authors.lastname: Kostka G
authors.forename: Elisabeth
authors.initials: E
authors.lastname: Ehler
authors.forename: Oliver
authors.initials: O
authors.lastname: Brandau
authors.forename: Reinhard
authors.initials: R
authors.lastname: Fässler
mesh_terms: D016475:3T3 Cells; D048868:Adaptor Proteins, Signal Transducing; D000818:Animals; D002352:Carrier Proteins / Q000378:metabolism; D002462:Cell Membrane / Q000378:metabolism*; D018076:DNA, Complementary / Q000032:analysis / Q000235:genetics; D004268:DNA-Binding Proteins / Q000235:genetics / Q000302:isolation & purification*; D004622:Embryo, Mammalian / Q000196:embryology / Q000378:metabolism; D005057:Eukaryotic Cells / Q000378:metabolism* / Q000648:ultrastructure; D005109:Extracellular Matrix / Q000378:metabolism* / Q000648:ultrastructure; D005333:Fetus; D005347:Fibroblasts / Q000378:metabolism; D022001:Focal Adhesions / Q000378:metabolism* / Q000648:ultrastructure; D060588:LIM Domain Proteins; D008565:Membrane Proteins; D051379:Mice; D008969:Molecular Sequence Data; D032383:Myocytes, Cardiac / Q000378:metabolism; D020033:Protein Isoforms / Q000235:genetics / Q000302:isolation & purification; D017346:Protein Serine-Threonine Kinases / Q000378:metabolism; D017434:Protein Structure, Tertiary / Q000235:genetics; D012333:RNA, Messenger / Q000378:metabolism; D017386:Sequence Homology, Amino Acid; D012689:Sequence Homology, Nucleic Acid; D014781:Viscera / Q000196:embryology / Q000378:metabolism; D000099200:Scaffold Protein ILK
chemical_list: D048868:Adaptor Proteins, Signal Transducing; D002352:Carrier Proteins; D018076:DNA, Complementary; D004268:DNA-Binding Proteins; D060588:LIM Domain Proteins; D008565:Membrane Proteins; D020033:Protein Isoforms; D017346:Protein Serine-Threonine Kinases; D012333:RNA, Messenger; D000099200:Scaffold Protein ILK; C490232:Lims1 protein, mouse