The DOI matches its Crossref record; 52 of the 52 references it cites were found in a registry or an index.
Determinants of specificity in TGF-β signal transduction
Open accessAbstract
Signal transduction by the TGF-β family involves sets of receptor serine/threonine kinases, Smad proteins that act as receptor substrates, and Smad-associated transcription factors that target specific genes. We have identified discrete structural elements that dictate the selective interactions between receptors and Smads and between Smads and transcription factors in the TGF-β and BMP pathways. A cluster of four residues in the L45 loop of the type I receptor kinase domain, and a matching set of two residues in the L3 loop of the Smad carboxy-terminal domain establish the specificity of receptor–Smad interactions. A cluster of residues in the highly exposed α-helix 2 of the Smad carboxy-terminal domain specify the interaction with the DNA-binding factor Fast1 and, as a result, the gene responses mediated by the pathway. By establishing specific interactions, these determinants keep the TGF-β and BMP pathways segregated from each other.
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Cites
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Self-citationTGF-β signalling from cell membrane to nucleus through SMAD proteins
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Self-citationSignaling Through Scaffold, Anchoring, and Adaptor Proteins
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Cited by
Hunter, T. (2000) · Cell · doi:10.1016/s0092-8674(00)81688-8 · Cited by 2,586
TGFβ Signaling in Growth Control, Cancer, and Heritable Disorders
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Self-citationSPECIFICITY AND VERSATILITY IN TGF-β SIGNALING THROUGH SMADS
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Mechanisms of specificity in protein phosphorylation
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Metadata
- Authors
- Chen, Y.-G., Hata, A., Lo, R. S., Wotton, D., Shi, Y., Pavletich, N., & Massagué, J.
- Venue
- Genes & Development
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 1998-07-15
- Volume
- 12
- Issue
- 14
- Pages
- 2144-2152
- ISSN
- 0890-9369 (ISSN-L)
- 1549-5477
- OpenAlex
- W2169237074
- Cited by
- 361
- References
- 52
- Type
- posted content
- Language
- en
- Open access
- diamond
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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