NDLI: The alternatively spliced acid box region plays a key role in FGF receptor autoinhibition.

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The alternatively spliced acid box region plays a key role in FGF receptor autoinhibition.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Kalinina, Juliya Dutta, Kaushik Ilghari, Dariush Beenken, Andrew Goetz, Regina Eliseenkova, Anna V. Cowburn, David Mohammadi, Moosa
Description	Country affiliation: United States Author Affiliation: Kalinina J ( Department of Pharmacology, New York University School of Medicine, 550, First Avenue, New York, NY 10016, USA.)
Abstract	Uncontrolled fibroblast growth factor (FGF) signaling can lead to human malignancies necessitating multiple layers of self-regulatory control mechanisms. Fibroblast growth factor receptor (FGFR) autoinhibition mediated by the alternatively spliced immunoglobulin (Ig) domain 1 (D1) and the acid box (AB)-containing linker between D1 and Ig domain 2 (D2) serves as the first line of defense to minimize inadvertent FGF signaling. In this report, nuclear magnetic resonance and surface plasmon resonance spectroscopy are used to demonstrate that the AB subregion of FGFR electrostatically engages the heparan sulfate (HS)-binding site on the D2 domain in cis to directly suppress HS-binding affinity of FGFR. Furthermore, the cis electrostatic interaction sterically autoinhibits ligand-binding affinity of FGFR because of the close proximity of HS-binding and primary ligand-binding sites on the D2 domain. These data, together with the strong amino acid sequence conservation of the AB subregion among FGFR orthologs, highlight the universal role of the AB subregion in FGFR autoinhibition.
File Format	HTM / HTML
ISSN	09692126
e-ISSN	18784186
DOI	10.1016/j.str.2011.10.022
Journal	Structure
Issue Number	1
Volume Number	20
Language	English
Publisher	Elsevier
Publisher Date	2012-01-11
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Discipline Molecular Biology Discipline Biochemistry Discipline Biotechnology Fibroblast Growth Factors Metabolism Models, Molecular Protein Structure, Tertiary Genetics Receptors, Fibroblast Growth Factor Signal Transduction Physiology Alternative Splicing Amino Acid Sequence Conserved Sequence Heparitin Sulfate Molecular Sequence Data Nuclear Magnetic Resonance, Biomolecular Protein Binding Static Electricity Surface Plasmon Resonance Research Support, N.i.h., Extramural
Content Type	Text
Resource Type	Article
Subject	Structural Biology Molecular Biology

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The Alternatively Spliced Acid Box Region Plays a Key Role in FGF Receptor Autoinhibition

Structure of the fibrillin-1 N-terminal domains suggests that heparan sulfate regulates the early stages of microfibril assembly.

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Insights into the molecular basis for fibroblast growth factor receptor autoinhibition and ligand-binding promiscuity.

Spatial and temporal expression of heparan sulfate in mouse development regulates FGF and FGF receptor assembly

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The alternatively spliced acid box region plays a key role in FGF receptor autoinhibition.

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The Alternatively Spliced Acid Box Region Plays a Key Role in FGF Receptor Autoinhibition

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