ArticleThe Journal of biological chemistry2015
Alternative binding modes identified for growth and differentiation factor-associated serum protein (GASP) family antagonism of myostatin.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- Characterization of tolloid-mediated cleavage of the GDF8 procomplex.The Biochemical journal · 2021Article
- Heparin-mediated dimerization of follistatin.Experimental biology and medicine (Maywood, N.J.) · 2021Article
- Similar sequences but dissimilar biological functions of GDF11 and myostatin.Experimental & molecular medicine · 2020Review
- Characterization of the different oligomeric states of the DAN family antagonists SOSTDC1 and SOST.The Biochemical journal · 2020Article
- Variation in zygotic CRISPR/Cas9 gene editing outcomes generates novel reporter and deletion alleles at the Gdf11 locus.Scientific reports · 2019Article
- Structural biology of the TGFβ family.Experimental biology and medicine (Maywood, N.J.) · 2019Review
- Crystal structure of the WFIKKN2 follistatin domain reveals insight into how it inhibits growth differentiation factor 8 (GDF8) and GDF11.The Journal of biological chemistry · 2019Article
- Beyond the Big Five: Investigating Myostatin Structure, Polymorphism and Expression inFrontiers in genetics · 2019Article
- Relationship of Circulating Growth and Differentiation Factors 8 and 11 and Their Antagonists as Measured Using Liquid Chromatography-Tandem Mass Spectrometry With Age and Skeletal Muscle Strength in Healthy Adults.The journals of gerontology. Series A, Biological sciences and medical sciences · 2019Article
- Structure of the human myostatin precursor and determinants of growth factor latency.The EMBO journal · 2018Article
- Molecular characterization of latent GDF8 reveals mechanisms of activation.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Structural basis for potency differences between GDF8 and GDF11.BMC biology · 2017Article
- Binding Properties of the Transforming Growth Factor-β Coreceptor Betaglycan: Proposed Mechanism for Potentiation of Receptor Complex Assembly and Signaling.Biochemistry · 2016Article
- Enhancement of C2C12 myoblast proliferation and differentiation by GASP-2, a myostatin inhibitor.Biochemistry and biophysics reports · 2016Article
- Biochemistry and Biology of GDF11 and Myostatin: Similarities, Differences, and Questions for Future Investigation.Circulation research · 2016Review
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
Myostatin, a member of the TGF-β family of ligands, is a strong negative regulator of muscle growth. As such, it is a prime therapeutic target for muscle wasting disorders. Similar to other TGF-β family ligands, myostatin is neutralized by binding one of a number of structurally diverse antagonists. Included are the antagonists GASP-1 and GASP-2, which are unique in that they specifically antagonize myostatin. However, little is known from a structural standpoint describing the interactions of GASP antagonists with myostatin. Here, we present the First low resolution solution structure of myostatin-free and myostatin-bound states of GASP-1 and GASP-2. Our studies have revealed GASP-1, which is 100 times more potent than GASP-2, preferentially binds myostatin in an asymmetrical 1:1 complex, whereas GASP-2 binds in a symmetrical 2:1 complex. Additionally, C-terminal truncations of GASP-1 result in less potent myostatin inhibitors that form a 2:1 complex, suggesting that the C-terminal domains of GASP-1 are the primary mediators for asymmetric complex formation. Overall, this study provides a new perspective on TGF-β antagonism, where closely related antagonists can utilize different ligand-binding strategies.
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