| 1995 |
Mutations in gamma-sarcoglycan (SGCG) not only abolish gamma-sarcoglycan but also disrupt the integrity of the entire sarcoglycan complex, establishing that gamma-sarcoglycan is required for complex integrity. |
Genetic mapping and mutation analysis in SCARMD patients combined with protein complex assessment |
Science |
High |
7481775
|
| 1996 |
Frameshifting mutations disrupting the distal carboxyl-terminus of gamma-sarcoglycan result in complete absence of both gamma- and beta-sarcoglycan, demonstrating that the C-terminal region (which contains EGF-like cysteine-rich sequences) is essential for stability of the sarcoglycan complex. |
Mutation analysis of patient muscle biopsies combined with immunostaining for sarcoglycan subunits |
Human molecular genetics |
Medium |
8923014
|
| 1996 |
Alpha-, beta-, and gamma-sarcoglycan constitute a tightly associated sarcolemmal complex that cannot be disrupted by SDS treatment, demonstrating their strong biochemical interdependence at the sarcolemma. |
Immunofluorescence, Western blotting, and SDS-resistance co-fractionation of the dystrophin-glycoprotein complex from skeletal muscle |
FEBS letters |
Medium |
8641426
|
| 1998 |
Genetic knockout of gamma-sarcoglycan in mice causes secondary reduction of beta- and delta-sarcoglycan with partial retention of alpha- and epsilon-sarcoglycan, indicating that beta-, gamma-, and delta-sarcoglycan function as a unit. Membrane disruptions and apoptosis occurred independently of dystrophin loss, demonstrating that sarcoglycan loss is itself sufficient to cause membrane defects. |
Homologous recombination knockout mouse; Evans blue dye vital staining; immunofluorescence; TUNEL apoptosis assay |
The Journal of cell biology |
High |
9732288
|
| 2000 |
Gamma-sarcoglycan is expressed in smooth muscle and associates with epsilon-, beta-, and delta-sarcoglycans and sarcospan to form the smooth muscle sarcoglycan-sarcospan complex, distinct from the striated muscle complex. |
Immunoblotting, co-immunoprecipitation/biochemical analysis of smooth muscle membranes, smooth muscle cell culture, and analysis of animal models and a patient with gamma-sarcoglycanopathy |
The Journal of biological chemistry |
Medium |
10993904
|
| 2001 |
Overexpression of gamma-sarcoglycan in mouse muscle leads to cytoplasmic aggregates that prevent normal membrane targeting, upregulation of alpha- and beta-sarcoglycan, and severe muscular dystrophy — demonstrating that proper dosage and membrane localization of gamma-sarcoglycan are critical for correct sarcoglycan complex assembly. |
Transgenic mouse overexpression under muscle creatine kinase promoter; histology; immunofluorescence; Western blotting |
The Journal of biological chemistry |
Medium |
11287429
|
| 2001 |
The gamma-sarcoglycan promoter contains a basal promoter region and two myogenesis-dependent enhancer regions; A/T-rich and E-box elements in the upstream enhancer are essential for activation after myotube formation, and MyoD acts as a trans-activator of gamma-sarcoglycan transcription. |
Reporter gene constructs with promoter deletions in C2C12 cells; co-transfection with MyoD expression vectors in 10T1/2 fibroblasts; electrophoretic mobility shift assay for binding protein identification |
European journal of biochemistry |
Medium |
11179961
|
| 2001 |
Delta- and gamma-sarcoglycans localize not only to the sarcolemma but also to the sarcoplasmic reticulum in skeletal muscle: delta-sarcoglycan is found in terminal cisternae, while gamma-sarcoglycan is found in both terminal cisternae and longitudinal SR over I-bands, suggesting functions independent of the dystrophin complex in the SR. |
Confocal microscopy and immunoelectron microscopy with subcellular marker co-labeling in rat and mouse skeletal muscle |
The journal of histochemistry and cytochemistry |
Medium |
11259456
|
| 2006 |
Biglycan physically binds to gamma-sarcoglycan (as well as alpha-sarcoglycan) via distinct sites on its polypeptide core, and is a component of the dystrophin glycoprotein complex isolated from skeletal muscle membranes. In biglycan-null mice, gamma-sarcoglycan expression is selectively reduced at early developmental stages (P14–P21), establishing biglycan as a ligand and developmental regulator of gamma-sarcoglycan. |
Ligand blot overlay, co-immunoprecipitation, biglycan-decorin chimeras, biochemical fractionation of skeletal muscle membranes, immunohistochemistry and Western blotting in biglycan-null mice |
Journal of cellular physiology |
Medium |
16883602
|
| 2006 |
Zeta-sarcoglycan can substitute for gamma-sarcoglycan in forming a sarcoglycan complex (alpha-beta-zeta-delta), demonstrating that gamma-sarcoglycan's structural role in complex formation can be fulfilled by its homolog zeta-sarcoglycan. |
Co-transfection of expression vectors for all six sarcoglycans and dystroglycan into CHO cells followed by immunoprecipitation analysis |
Experimental cell research |
Medium |
16635485
|
| 2010 |
Tyrosine 6 (Tyr6) in the intracellular domain of gamma-sarcoglycan is not required for sarcolemmal localization, but is required for normal ERK1/2 phosphorylation signaling after eccentric contractions — demonstrating that localization and mechanical signal transduction are molecularly separable functions of gamma-sarcoglycan. |
Viral-mediated gene transfer of wild-type and Y6A mutant gamma-sarcoglycan into gsg-/- mouse muscle; immunofluorescence for localization; immunoblotting for ERK1/2 phosphorylation after eccentric contractions |
The Journal of biological chemistry |
High |
20371873
|
| 2014 |
Loss of gamma-sarcoglycan elevates basal p70S6K activation in skeletal muscle in a calcium-independent manner and causes sustained (rather than transient) p70S6K activation after stretch; rapamycin blocks p70S6K but cannot normalize downstream S6RP phosphorylation in gamma-SG-null muscle, indicating gamma-sarcoglycan is required for proper inactivation of the mTOR/p70S6K mechanotransduction pathway. |
Cyclic passive stretch of C2C12 myotubes, primary cultures and isolated muscles from C57 and gamma-SG-null mice; immunoblotting for phosphorylated signaling proteins; rapamycin and calcium-chelation pharmacological experiments |
Skeletal muscle |
Medium |
25024843
|
| 2015 |
Gamma-sarcoglycan interacts with the muscle-specific protein archvillin (identified by yeast two-hybrid), and loss of gamma-sarcoglycan causes archvillin upregulation and delocalization at the sarcolemma as well as ablation of the mechanically stimulated archvillin–P-ERK1/2 association, positioning archvillin as a mechanically sensitive signaling component downstream of gamma-sarcoglycan. |
Yeast two-hybrid screen; immunofluorescence and Western blotting in gsg-/- and mdx mouse muscle; rAAV rescue experiments; in situ eccentric contractions with P-ERK1/2 nuclear activation analysis; co-immunoprecipitation of archvillin with P-ERK1/2 |
Human molecular genetics |
Medium |
25605665
|
| 2019 |
Full-length recombinant gamma-sarcoglycan (SGCG) was expressed, purified, and subjected to solution NMR spectroscopy in detergent environments, yielding the first NMR spectra of the full-length membrane glycoprotein and providing initial structural characterization. |
Recombinant expression in E. coli inclusion bodies using TrpΔLE fusion; chemical cleavage; size-exclusion chromatography; SDS-PAGE; mass spectrometry; 15N-labeled solution NMR spectroscopy |
Protein expression and purification |
Medium |
31682967
|
| 2022 |
Proteomic analysis of gamma-sarcoglycan immunoprecipitates from sarcolemmal fractions identified NKCC1 (SLC12A2) as a novel gamma-sarcoglycan complex-associated protein; NKCC1 co-localizes with gamma-sarcoglycan upon co-expression in RH30 cells and co-immunoprecipitates via its cytosolic domains. Pharmacological inhibition of NKCC1 with bumetanide reduces strain-induced ERK1/2 phosphorylation in isolated muscles, linking NKCC1 to gamma-sarcoglycan-dependent mechanosignaling. |
LC-MS/MS proteomics of anti-Sgcg immunoprecipitates from enriched sarcolemmal fractions; co-expression and co-immunoprecipitation in RH30 rhabdomyosarcoma cells; immunofluorescence co-localization; bumetanide pharmacological inhibition with ERK1/2 phosphorylation readout in isolated muscles |
Skeletal muscle |
Medium |
35065666
|
| 2023 |
Gamma-sarcoglycan incorporated into nanodiscs can undergo N-linked glycosylation in vitro by enzymatic transfer of sugar to an asparagine residue, demonstrating that this post-translational modification can be reconstituted in a lipid bilayer environment. |
Nanodisc reconstitution with long-chain lipids and membrane scaffold proteins; in vitro N-linked glycosylation assay with oligosaccharyltransferase; SDS-PAGE and mass spectrometry validation |
ACS omega |
Medium |
37929139
|
| 2010 |
In delta-sarcoglycan knockout mice, gamma-sarcoglycan expression is secondarily reduced in both transverse tubule and sarcoplasmic reticulum membranes, demonstrating that delta-sarcoglycan stabilizes gamma-sarcoglycan in these intracellular membrane compartments. |
Immunoblotting of purified TT and SR membrane fractions from wild-type and delta-SG knockout mice |
Cell calcium |
Low |
20638123
|