Structural insights into BMP receptors: Specificity, activation and inhibition

Yadin, David; Knaus, Petra; Mueller, Thomas D.

doi:10.1016/j.cytogfr.2015.11.005

Cited by 189 publications

(229 citation statements)

References 213 publications

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“…Consistent with this structure, MSTN prodomain residues 43-115 are necessary and sufficient to inhibit ligand activity 43, 44 . Interestingly, this region contains the TLD proteolytic site 17,18 and is highly conserved with GDF11, suggesting that it serves a similar role in regulating GDF11 (Fig. 3B).…”

Section: Biochemical Regulation Of Gdf11 and Myostatinmentioning

confidence: 99%

“…1A). The mature ligands are propeller-shaped, disulfide-linked dimers that initiate signal transduction by engaging two Type II receptors and two Type I receptors using convex and concave surfaces, respectively 18 (Fig. 2).…”

Section: Biochemical Regulation Of Gdf11 and Myostatinmentioning

confidence: 99%

“…Unlike the BMPs, the TGFβ and activin/MSTN sub-classes exhibit high affinity for the Type II receptor and low affinity for the Type I receptor 18 . The Type II receptors for the BMP and activin sub-classes bind on the concave surface of the fingers whereas TGFβs bind the Type II receptor more distally, towards the fingertips 18 .…”

Section: Biochemical Regulation Of Gdf11 and Myostatinmentioning

confidence: 99%

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Biochemistry and Biology of GDF11 and Myostatin

Walker

Poggioli

Katsimpardi³

et al. 2016

Circulation Research

167

106

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Growth differentiation factor 11 (GDF11) and myostatin (or GDF8) are closely related members of the transforming growth factor β superfamily and are often perceived to serve similar or overlapping roles. Yet, despite commonalities in protein sequence, receptor utilization and signaling, accumulating evidence suggests that these 2 ligands can have distinct functions in many situations. GDF11 is essential for mammalian development and has been suggested to regulate aging of multiple tissues, whereas myostatin is a well-described negative regulator of postnatal skeletal and cardiac muscle mass and modulates metabolic processes. In this review, we discuss the biochemical regulation of GDF11 and myostatin and their functions in the heart, skeletal muscle, and brain. We also highlight recent clinical findings with respect to a potential role for GDF11 and/or myostatin in humans with heart disease. Finally, we address key outstanding questions related to GDF11 and myostatin dynamics and signaling during development, growth, and aging. (Circ Res.

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Section: Biochemical Regulation Of Gdf11 and Myostatinmentioning

confidence: 99%

Section: Biochemical Regulation Of Gdf11 and Myostatinmentioning

confidence: 99%

Section: Biochemical Regulation Of Gdf11 and Myostatinmentioning

confidence: 99%

See 1 more Smart Citation

Biochemistry and Biology of GDF11 and Myostatin

Walker

Poggioli

Katsimpardi³

et al. 2016

Circulation Research

167

106

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“…A major effect of dorsomorphin lies in the dose-dependent inhibition of SMAD1/5/8 phosphorylation, inhibiting IRF1-dependent gene transcription (45). This signaling pathway is triggered by the bone morphogenetic proteins, specifically BMP4 (46,47). Consequently, we investigated the impact of dorsomorphin on p-SMAD1/5 and IRF1 in CAD macrophages (Figure 8, C-E).…”

Section: 8mentioning

confidence: 99%

Pyruvate controls the checkpoint inhibitor PD-L1 and suppresses T cell immunity

Watanabe

Shirai

Namkoong

et al. 2017

Journal of Clinical Investigation

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“…The intricate oligomerisation processes differ depending on the individual growth factor ligand. There exists a wealth of data on ligand-receptor interactions and subsequent signalling pathways, which are summarised in reviews by (Wu and Hill, 2009;Hinck, 2012;Macias et al, 2015;Yadin et al, 2016).…”

Section: Growth Factors Of the Tgf-β/bmp Family Tgf-β Structure Supermentioning

confidence: 99%

Cystine knot growth factors and their functionally versatile proregions

Schwarz

2017

Biological Chemistry

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Abstract:The cystine knot disulfide pattern has been found to be widespread in nature, since it has been detected in proteins from plants, marine snails, spiders and mammals. Cystine knot proteins are secreted proteins. Their functions range from defense mechanisms as toxins, e.g. ion channel or enzyme inhibitors, to hormones, blood factors and growth factors. Cystine knot proteins can be divided into two superordinate groups. (i) The cystine knot peptides, also referred to -with other non-cystine knot proteins -as knottins, with linear and cyclic polypeptide chains. (ii) The cystine knot growth factor family, which is in the focus of this article. The disulfide ring structure of the cystine knot peptides is made up by the half-cystines 1-4 and 2-5, and the threading disulfide bond is formed by the half-cystines, 3-6. In the growth factor group, the disulfides of half-cystines 1 and 4 pass the ring structure formed by the half-cystines 2-5 and 3-6. In this review, special emphasis will be devoted to the growth factor cystine knot proteins and their proregions. The latter have shifted into the focus of scientific interest as their important biological roles are just to be unravelled.

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Structural insights into BMP receptors: Specificity, activation and inhibition

Cited by 189 publications

References 213 publications

Biochemistry and Biology of GDF11 and Myostatin

Biochemistry and Biology of GDF11 and Myostatin

Pyruvate controls the checkpoint inhibitor PD-L1 and suppresses T cell immunity

Cystine knot growth factors and their functionally versatile proregions

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