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MALS is a binding partner of IRSp53 at cell–cell contacts
Author(s) -
Hori Kei,
Konno Daijiro,
Maruoka Hisato,
Sobue Kenji
Publication year - 2003
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(03)01074-3
Subject(s) - pdz domain , microbiology and biotechnology , cytoskeleton , cdc42 , actin cytoskeleton , lamellipodium , cell membrane , actin , biophysics , immunoprecipitation , cell , cell migration , rac gtp binding proteins , chemistry , biology , cell culture , biochemistry , genetics
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.