Affixin activates Rac1 via βPIX in C2C12 myoblast

Affixin/β-parvin is an integrin-linked kinase (ILK)-binding focal adhesion protein highly expressed in skeletal muscle and heart. To elucidate the possible role of affixin in skeletal muscle, we established stable C2C12 cell line expressing T7-tagged human affixin (C2C12-affixin cells). Exogenous ex...

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Published inFEBS letters Vol. 582; no. 8; pp. 1189 - 1196
Main Authors Matsuda, Chie, Kameyama, Kimihiko, Suzuki, Atsushi, Mishima, Wataru, Yamaji, Satoshi, Okamoto, Harumasa, Nishino, Ichizo, Hayashi, Yukiko K.
Format Journal Article
LanguageEnglish
Published Elsevier B.V 09.04.2008
Subjects
Affixin/β-parvin
C2C12-affixin
caponin-homology
Chinese hamster ovary
CHO
Cytoskeletal actin
Dbl-homology
GEF
GST
guanine nucleotide exchange factor
gulutathione S-transferase
ILK
integrin-linked kinase
Lamellipodia
p21-activated kinase
PAK
PAK-interactive exchange factor
PIX
pleckstrin-homology
stable C2C12 cell line expressing T7-tagged human affixin
βPIX
βPIX
DH
CH
ILK
GEF
GST
CHO
C2C12-affixin
Affixin/β-parvin
Lamellipodia
PH
PAK
Cytoskeletal actin
PIX
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Abstract Affixin/β-parvin is an integrin-linked kinase (ILK)-binding focal adhesion protein highly expressed in skeletal muscle and heart. To elucidate the possible role of affixin in skeletal muscle, we established stable C2C12 cell line expressing T7-tagged human affixin (C2C12-affixin cells). Exogenous expression of affixin promotes lamellipodium formation where affixin, ILK αp21-activated kinase (PAK)-interactive exchange factor (PIX) and βPIX accumulate. The association of affixin and βPIX was confirmed by immunoprecipitation and pull down assay. In C2C12-affixin cells, an increased level of activated Rac1 but not Cdc42 was observed, and mutant βPIX lacking guanine nucleotide exchange factor activity inhibited lamellipodium formation. These results suggest that affixin is involved in reorganization of subsarcolemmal cytoskeletal actin by activation of Rac1 through α and βPIXs in skeletal muscle. MINT-6179203, MINT-6179212, MINT-6178859, MINT-6178812, MINT-6178832, MINT-6178843:Affixin (uniprotkb:Q9HBI1) physically interacts (MI:0218) with βpix (uniprotkb:Q9ES28) by coimmunoprecipitation (MI:0019)MINT-6179221:Affixin (uniprotkb:Q9HBI1) physically interacts (MI:0218) with αpix (uniprotkb:Q8K4I3) by coimmunoprecipitation (MI:0019)MINT-6178962, MINT-6178983:Affixin (uniprotkb:Q9HBI1) physically interacts (MI:0218) with βpix (uniprotkb:Q9ES28) by pull-down (MI:0096)MINT-6179002, MINT-6179021:Affixin (uniprotkb:Q9HBI1) binds (MI:0407) βpix (uniprotkb:Q9ES28) by pull-down (MI:0096)MINT-6179039:PAK1 (uniprotkb:Q13153) physically interacts (MI:0218) with Rac1 (uniprotkb:P63001) by pull-down (MI:0096)MINT-6179054:PAK1 (uniprotkb:Q13153) physically interacts (MI:0218) with Cdc42 (uniprotkb:P70766) by pull-down (MI:0096)MINT-6178790:Affixin (uniprotkb:Q9HBI1) and αpix (uniprotkb:Q8K4I3) colocalize (MI:0403) by fluorescence microscopy (MI:0416)MINT-6178760:Affixin (uniprotkb:Q9HBI1) and βpix (uniprotkb:Q9ES28) colocalize (MI:0403) by fluorescence microscopy (MI:0416)MINT-6178801:Affixin (uniprotkb:Q9HBI1) and dysferlin (uniprotkb:Q9ESD7) colocalize (MI:0403) by fluorescence microscopy (MI:0416)MINT-6178779:Affixin (uniprotkb:Q9HBI1) and ILK (uniprotkb:O55222) colocalize (MI:0403) by fluorescence microscopy (MI:0416)
AbstractList Affixin/β-parvin is an integrin-linked kinase (ILK)-binding focal adhesion protein highly expressed in skeletal muscle and heart. To elucidate the possible role of affixin in skeletal muscle, we established stable C2C12 cell line expressing T7-tagged human affixin (C2C12-affixin cells). Exogenous expression of affixin promotes lamellipodium formation where affixin, ILK αp21-activated kinase (PAK)-interactive exchange factor (PIX) and βPIX accumulate. The association of affixin and βPIX was confirmed by immunoprecipitation and pull down assay. In C2C12-affixin cells, an increased level of activated Rac1 but not Cdc42 was observed, and mutant βPIX lacking guanine nucleotide exchange factor activity inhibited lamellipodium formation. These results suggest that affixin is involved in reorganization of subsarcolemmal cytoskeletal actin by activation of Rac1 through α and βPIXs in skeletal muscle. MINT-6179203, MINT-6179212, MINT-6178859, MINT-6178812, MINT-6178832, MINT-6178843:Affixin (uniprotkb:Q9HBI1) physically interacts (MI:0218) with βpix (uniprotkb:Q9ES28) by coimmunoprecipitation (MI:0019)MINT-6179221:Affixin (uniprotkb:Q9HBI1) physically interacts (MI:0218) with αpix (uniprotkb:Q8K4I3) by coimmunoprecipitation (MI:0019)MINT-6178962, MINT-6178983:Affixin (uniprotkb:Q9HBI1) physically interacts (MI:0218) with βpix (uniprotkb:Q9ES28) by pull-down (MI:0096)MINT-6179002, MINT-6179021:Affixin (uniprotkb:Q9HBI1) binds (MI:0407) βpix (uniprotkb:Q9ES28) by pull-down (MI:0096)MINT-6179039:PAK1 (uniprotkb:Q13153) physically interacts (MI:0218) with Rac1 (uniprotkb:P63001) by pull-down (MI:0096)MINT-6179054:PAK1 (uniprotkb:Q13153) physically interacts (MI:0218) with Cdc42 (uniprotkb:P70766) by pull-down (MI:0096)MINT-6178790:Affixin (uniprotkb:Q9HBI1) and αpix (uniprotkb:Q8K4I3) colocalize (MI:0403) by fluorescence microscopy (MI:0416)MINT-6178760:Affixin (uniprotkb:Q9HBI1) and βpix (uniprotkb:Q9ES28) colocalize (MI:0403) by fluorescence microscopy (MI:0416)MINT-6178801:Affixin (uniprotkb:Q9HBI1) and dysferlin (uniprotkb:Q9ESD7) colocalize (MI:0403) by fluorescence microscopy (MI:0416)MINT-6178779:Affixin (uniprotkb:Q9HBI1) and ILK (uniprotkb:O55222) colocalize (MI:0403) by fluorescence microscopy (MI:0416)
— MINT‐6179203, MINT‐6179212, MINT‐6178859, MINT‐6178812, MINT‐6178832, MINT‐6178843: Affixin (uniprotkb:Q9HBI1) physically interacts (MI:0218) with βpix (uniprotkb:Q9ES28) by coimmunoprecipitation (MI:0019) — MINT‐6179221: Affixin (uniprotkb:Q9HBI1) physically interacts (MI:0218) with αpix (uniprotkb:Q8K4I3) by coimmunoprecipitation (MI:0019) — MINT‐6178962, MINT‐6178983: Affixin (uniprotkb:Q9HBI1) physically interacts (MI:0218) with βpix (uniprotkb:Q9ES28) by pull-down (MI:0096) — MINT‐6179002, MINT‐6179021: Affixin (uniprotkb:Q9HBI1) binds (MI:0407) βpix (uniprotkb:Q9ES28) by pull-down (MI:0096) — MINT‐6179039: PAK1 (uniprotkb:Q13153) physically interacts (MI:0218) with Rac1 (uniprotkb:P63001) by pull-down (MI:0096) — MINT‐6179054: PAK1 (uniprotkb:Q13153) physically interacts (MI:0218) with Cdc42 (uniprotkb:P70766) by pull-down (MI:0096) — MINT‐6178790: Affixin (uniprotkb:Q9HBI1) and αpix (uniprotkb:Q8K4I3) colocalize (MI:0403) by fluorescence microscopy (MI:0416) — MINT‐6178760: Affixin (uniprotkb:Q9HBI1) and βpix (uniprotkb:Q9ES28) colocalize (MI:0403) by fluorescence microscopy (MI:0416) — MINT‐6178801: Affixin (uniprotkb:Q9HBI1) and dysferlin (uniprotkb:Q9ESD7) colocalize (MI:0403) by fluorescence microscopy (MI:0416) — MINT‐6178779: Affixin (uniprotkb:Q9HBI1) and ILK (uniprotkb:O55222) colocalize (MI:0403) by fluorescence microscopy (MI:0416)
Author Suzuki, Atsushi
Kameyama, Kimihiko
Mishima, Wataru
Yamaji, Satoshi
Matsuda, Chie
Okamoto, Harumasa
Nishino, Ichizo
Hayashi, Yukiko K.
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  surname: Matsuda
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  organization: Neuroscience Research Institute, AIST, Central 6, 1-1-1 Higashi, Tsukuba, Ibaraki 305-8566, Japan
– sequence: 2
  givenname: Kimihiko
  surname: Kameyama
  fullname: Kameyama, Kimihiko
  organization: Neuroscience Research Institute, AIST, Central 6, 1-1-1 Higashi, Tsukuba, Ibaraki 305-8566, Japan
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  givenname: Atsushi
  surname: Suzuki
  fullname: Suzuki, Atsushi
  organization: Department of Molecular Biology, Yokohama City University, Graduate School of Medicine, 3-9 Fukuura, Kanazawa-ku, Yokohama 236-0004, Japan
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  givenname: Wataru
  surname: Mishima
  fullname: Mishima, Wataru
  organization: Department of Internal Medicine and Clinical Immunology, Yokohama City University, Graduate School of Medicine, 3-9 Fukuura, Kanazawa-ku, Yokohama 236-0004, Japan
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  givenname: Satoshi
  surname: Yamaji
  fullname: Yamaji, Satoshi
  organization: Department of Internal Medicine and Clinical Immunology, Yokohama City University, Graduate School of Medicine, 3-9 Fukuura, Kanazawa-ku, Yokohama 236-0004, Japan
– sequence: 6
  givenname: Harumasa
  surname: Okamoto
  fullname: Okamoto, Harumasa
  organization: Neuroscience Research Institute, AIST, Central 6, 1-1-1 Higashi, Tsukuba, Ibaraki 305-8566, Japan
– sequence: 7
  givenname: Ichizo
  surname: Nishino
  fullname: Nishino, Ichizo
  organization: Department of Neuromuscular Research, National Institute of Neuroscience, NCNP, Ogawa-Higashi, Kodaira, Tokyo 187-8502, Japan
– sequence: 8
  givenname: Yukiko K.
  surname: Hayashi
  fullname: Hayashi, Yukiko K.
  organization: Department of Neuromuscular Research, National Institute of Neuroscience, NCNP, Ogawa-Higashi, Kodaira, Tokyo 187-8502, Japan
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Copyright 2008 Federation of European Biochemical Societies
FEBS Letters 582 (2008) 1873-3468 © 2015 Federation of European Biochemical Societies
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Issue 8
Keywords βPIX
DH
CH
ILK
GEF
GST
CHO
C2C12-affixin
Affixin/β-parvin
Lamellipodia
PH
PAK
Cytoskeletal actin
PIX
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Snippet Affixin/β-parvin is an integrin-linked kinase (ILK)-binding focal adhesion protein highly expressed in skeletal muscle and heart. To elucidate the possible...
— MINT‐6179203, MINT‐6179212, MINT‐6178859, MINT‐6178812, MINT‐6178832, MINT‐6178843: Affixin (uniprotkb:Q9HBI1) physically interacts (MI:0218) with βpix...
SourceID crossref
wiley
elsevier
SourceType Aggregation Database
Publisher
StartPage 1189
SubjectTerms Affixin/β-parvin
C2C12-affixin
caponin-homology
Chinese hamster ovary
CHO
Cytoskeletal actin
Dbl-homology
GEF
GST
guanine nucleotide exchange factor
gulutathione S-transferase
ILK
integrin-linked kinase
Lamellipodia
p21-activated kinase
PAK
PAK-interactive exchange factor
PIX
pleckstrin-homology
stable C2C12 cell line expressing T7-tagged human affixin
βPIX
Title Affixin activates Rac1 via βPIX in C2C12 myoblast
URI https://dx.doi.org/10.1016/j.febslet.2008.01.064
https://onlinelibrary.wiley.com/doi/abs/10.1016%2Fj.febslet.2008.01.064
Volume 582
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