Tensin stabilizes integrin adhesive contacts in Drosophila.
We report the functional characterization of the Drosophila ortholog of tensin, a protein implicated in linking integrins to the cytoskeleton and signaling pathways. A tensin null was generated and is viable with wing blisters, a phenotype characteristic of loss of integrin adhesion. In tensin mutants, mechanical abrasion is required during wing expansion to cause wing blisters, suggesting that tensin strengthens integrin adhesion. The localization of tensin requires integrins, talin, and integrin-linked kinase. The N-terminal domain and C-terminal PTB domain of tensin provide essential recruitment signals. The intervening SH2 domain is not localized on its own. We suggest a model where tensin is recruited to sites of integrin adhesion via its PTB and N-terminal domains, localizing the SH2 domain so that it can interact with phosphotyrosine-containing proteins, which stabilize the integrin link to the cytoskeleton.
Torgler
Catherine N
CN
Wellcome Trust/Cancer Research UK Gurdon Institute and Department of Anatomy, University of Cambridge, Tennis Court Road, Cambridge CB2 1QR, United Kingdom.
Narasimha
Maithreyi
M
Knox
Andrea L
AL
Zervas
Christos G
CG
Vernon
Matthew C
MC
Brown
Nicholas H
NH
D000818:Animals; D030801:Animals, Genetically Modified; D002448:Cell Adhesion / Q000235:genetics / Q000502:physiology*; D003599:Cytoskeleton / Q000378:metabolism; D004330:Drosophila / Q000235:genetics; D004625:Embryo, Nonmammalian; D051416:Focal Adhesion Protein-Tyrosine Kinases; D015870:Gene Expression; D018507:Gene Expression Regulation, Developmental; D017344:Genes, Insect / Q000235:genetics; D049452:Green Fluorescent Proteins; D007150:Immunohistochemistry / Q000379:methods; D017403:In Situ Hybridization / Q000379:methods; D019476:Insect Proteins / Q000378:metabolism; D016023:Integrins / Q000235:genetics / Q000502:physiology*; D007814:Larva; D008164:Luminescent Proteins / Q000378:metabolism; D008840:Microfilament Proteins / Q000235:genetics / Q000502:physiology*; D008954:Models, Biological; D009154:Mutation; D019000:Phosphotyrosine / Q000378:metabolism; D038941:Polypyrimidine Tract-Binding Protein; D011485:Protein Binding; D017346:Protein Serine-Threonine Kinases / Q000502:physiology; D011505:Protein-Tyrosine Kinases / Q000378:metabolism; D012333:RNA, Messenger / Q000096:biosynthesis; D020133:Reverse Transcriptase Polymerase Chain Reaction / Q000379:methods; D013312:Stress, Physiological / Q000235:genetics / Q000378:metabolism; D016608:Talin / Q000502:physiology; D000070876:Tensins; D014443:Tyrosine / Q000378:metabolism; D014921:Wings, Animal / Q000196:embryology / Q000378:metabolism; D018909:src Homology Domains / Q000502:physiology; D000099200:Scaffold Protein ILK
D051416:Focal Adhesion Protein-Tyrosine Kinases; D049452:Green Fluorescent Proteins; D019476:Insect Proteins; D016023:Integrins; D008164:Luminescent Proteins; D008840:Microfilament Proteins; D019000:Phosphotyrosine; D038941:Polypyrimidine Tract-Binding Protein; D017346:Protein Serine-Threonine Kinases; D011505:Protein-Tyrosine Kinases; D012333:RNA, Messenger; D016608:Talin; D000070876:Tensins; D014443:Tyrosine; D000099200:Scaffold Protein ILK