Syntrophin is an actin-binding protein the cellular localization of which is regulated through cytoskeletal reorganization in skeletal muscle cells

2004 ◽  
Vol 83 (10) ◽  
pp. 555-565 ◽  
Author(s):  
Yuko Iwata ◽  
Maurilio Sampaolesi ◽  
Munekazu Shigekawa ◽  
Shigeo Wakabayashi
Keyword(s):  
Skeletal Muscle ◽  
Cellular Localization ◽  
Binding Protein ◽  
Muscle Cells ◽  
Skeletal Muscle Cells ◽  
Actin Binding ◽  
Cytoskeletal Reorganization ◽  
Actin Binding Protein

scholarly journals Nexilin, a Cardiomyopathy-Associated F-Actin Binding Protein, Binds and Regulates IRS1 Signaling in Skeletal Muscle Cells

PLoS ONE ◽  
2013 ◽  
Vol 8 (1) ◽  
pp. e55634 ◽  
Author(s):  
Andrew Lee ◽  
Fumihiko Hakuno ◽  
Paul Northcott ◽  
Jeffrey E. Pessin ◽  
Maria Rozakis Adcock
Keyword(s):  
Skeletal Muscle ◽  
Binding Protein ◽  
Muscle Cells ◽  
Skeletal Muscle Cells ◽  
Actin Binding ◽  
Actin Binding Protein

scholarly journals Induction of utrophin gene expression by heregulin in skeletal muscle cells: Role of the N-box motif and GA binding protein

1999 ◽  
Vol 96 (6) ◽  
pp. 3223-3227 ◽  
Author(s):  
A. O. Gramolini ◽  
L. M. Angus ◽  
L. Schaeffer ◽  
E. A. Burton ◽  
J. M. Tinsley ◽  
...  
Keyword(s):  
Gene Expression ◽  
Skeletal Muscle ◽  
Binding Protein ◽  
Muscle Cells ◽  
Skeletal Muscle Cells ◽  
Ga Binding Protein

scholarly journals ECC meets CEU—New focus on the backdoor for calcium ions in skeletal muscle cells

2020 ◽  
Vol 152 (10) ◽  
Author(s):  
Werner Melzer
Keyword(s):  
Skeletal Muscle ◽  
Calcium Ions ◽  
Muscle Activity ◽  
Binding Protein ◽  
Muscle Cells ◽  
Skeletal Muscle Cells ◽  
Fast Skeletal Muscle

In this issue, Michelucci et al. report the existence of specific sites acting as Ca2+ entry units (CEUs) in fast skeletal muscle of mice lacking calsequestrin (CASQ1), the major Ca2+ binding protein of the SR. The CEU provides constitutive and store-operated Ca2+ entry (SOCE) and resistance to force decline resulting from SR Ca2+ depletion during repetitive muscle activity.

scholarly journals The PDZ Domain of the LIM Protein Enigma Binds to β-Tropomyosin

1999 ◽  
Vol 10 (6) ◽  
pp. 1973-1984 ◽  
Author(s):  
Pamela M. Guy ◽  
Daryn A. Kenny ◽  
Gordon N. Gill
Keyword(s):  
Skeletal Muscle ◽  
Family Member ◽  
Actin Filaments ◽  
Binding Protein ◽  
Pdz Domain ◽  
Actin Binding ◽  
C2c12 Myotubes ◽  
Lim Protein ◽  
Actin Binding Protein ◽  
Lim Domains

PDZ and LIM domains are modular protein interaction motifs present in proteins with diverse functions. Enigma is representative of a family of proteins composed of a series of conserved PDZ and LIM domains. The LIM domains of Enigma and its most related family member, Enigma homology protein, bind to protein kinases, whereas the PDZ domains of Enigma and family member actin-associated LIM protein bind to actin filaments. Enigma localizes to actin filaments in fibroblasts via its PDZ domain, and actin-associated LIM protein binds to and colocalizes with the actin-binding protein α-actinin-2 at Z lines in skeletal muscle. We show that Enigma is present at the Z line in skeletal muscle and that the PDZ domain of Enigma binds to a skeletal muscle target, the actin-binding protein tropomyosin (skeletal β-TM). The interaction between Enigma and skeletal β-TM was specific for the PDZ domain of Enigma, was abolished by mutations in the PDZ domain, and required the PDZ-binding consensus sequence (Thr-Ser-Leu) at the extreme carboxyl terminus of skeletal β-TM. Enigma interacted with isoforms of tropomyosin expressed in C2C12 myotubes and formed an immunoprecipitable complex with skeletal β-TM in transfected cells. The association of Enigma with skeletal β-TM suggests a role for Enigma as an adapter protein that directs LIM-binding proteins to actin filaments of muscle cells.

IRSp53 is a novel interactor of SHIP2: A role of the actin binding protein Mena in their cellular localization in breast cancer cells

2020 ◽  
Vol 73 ◽  
pp. 109692
Author(s):  
Mathieu Antoine ◽  
Isabelle Vandenbroere ◽  
Somadri Ghosh ◽  
Christophe Erneux ◽  
Isabelle Pirson
Keyword(s):  
Breast Cancer ◽  
Cancer Cells ◽  
Breast Cancer Cells ◽  
Cellular Localization ◽  
Binding Protein ◽  
Actin Binding ◽  
Actin Binding Protein
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