MALS is a binding partner of IRSp53 at cell–cell contacts

FEBS Letters

Konno, Daijiro¹  Sobue, Kenji¹  Hori, Kei¹  Maruoka, Hisato¹ 

[1] Department of Neuroscience (D13), Osaka University Graduate School of Medicine, Yamadaoka 2-2, Suita City, Osaka, Japan

关键词: PDZ domain;    Actin modulator;    Membrane cytoskeleton;    Epithelial cell;    IRSp53S;    insulin receptor substrate p53 short form;    PDZ domain;    PSD-95/Disc large/ZO-1 homology domain;    MALS;    mammalian Lin-7 homologue;   

DOI  :  10.1016/S0014-5793(03)01074-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Insulin receptor substrate p53 (IRSp53) is a key player in cytoskeletal dynamics, interacting with the actin modulators WAVE2 and Mena. Here, we identified a PDZ protein, MALS, as an IRSp53-interacting protein using a yeast two-hybrid screen. A pull-down assay showed that IRSp53 and MALS interact through the PDZ domain of MALS and the C-terminal PDZ-binding sequence of IRSp53. Their interaction in MDCK cells was also demonstrated by co-immunoprecipitation. Immunocytochemistry showed the colocalization of IRSp53 and MALS at cell–cell contacts. Cytochalasin D induced the redistribution of both proteins to the cytosol. Thus, MALS is a partner of IRSp53 anchoring the actin-based membrane cytoskeleton at cell–cell contacts.

【 授权许可】

Unknown