BIOMAT Database Logo BIOMAT Database Logo

Neurofibromin Structure, Functions and Regulation. 2020

Mohammed Bergoug, and Michel Doudeau, and Fabienne Godin, and Christine Mosrin, and Béatrice Vallée, and Hélène Bénédetti
Centre de Biophysique Moléculaire, CNRS, UPR 4301, University of Orléans and INSERM, CEDEX 2, 45071 Orléans, France.

Neurofibromin is a large and multifunctional protein encoded by the tumor suppressor gene NF1, mutations of which cause the tumor predisposition syndrome neurofibromatosis type 1 (NF1). Over the last three decades, studies of neurofibromin structure, interacting partners, and functions have shown that it is involved in several cell signaling pathways, including the Ras/MAPK, Akt/mTOR, ROCK/LIMK/cofilin, and cAMP/PKA pathways, and regulates many fundamental cellular processes, such as proliferation and migration, cytoskeletal dynamics, neurite outgrowth, dendritic-spine density, and dopamine levels. The crystallographic structure has been resolved for two of its functional domains, GRD (GAP-related (GTPase-activating protein) domain) and SecPH, and its post-translational modifications studied, showing it to be localized to several cell compartments. These findings have been of particular interest in the identification of many therapeutic targets and in the proposal of various therapeutic strategies to treat the symptoms of NF1. In this review, we provide an overview of the literature on neurofibromin structure, function, interactions, and regulation and highlight the relationships between them.

UI MeSH Term Description Entries
D011499 Protein Processing, Post-Translational Any of various enzymatically catalyzed post-translational modifications of PEPTIDES or PROTEINS in the cell of origin. These modifications include carboxylation; HYDROXYLATION; ACETYLATION; PHOSPHORYLATION; METHYLATION; GLYCOSYLATION; ubiquitination; oxidation; proteolysis; and crosslinking and result in changes in molecular weight and electrophoretic motility. Amino Acid Modification, Post-Translational,Post-Translational Modification,Post-Translational Protein Modification,Posttranslational Modification,Protein Modification, Post-Translational,Amino Acid Modification, Posttranslational,Post-Translational Amino Acid Modification,Post-Translational Modifications,Post-Translational Protein Processing,Posttranslational Amino Acid Modification,Posttranslational Modifications,Posttranslational Protein Processing,Protein Processing, Post Translational,Protein Processing, Posttranslational,Amino Acid Modification, Post Translational,Modification, Post-Translational,Modification, Post-Translational Protein,Modification, Posttranslational,Modifications, Post-Translational,Modifications, Post-Translational Protein,Modifications, Posttranslational,Post Translational Amino Acid Modification,Post Translational Modification,Post Translational Modifications,Post Translational Protein Modification,Post Translational Protein Processing,Post-Translational Protein Modifications,Processing, Post-Translational Protein,Processing, Posttranslational Protein,Protein Modification, Post Translational,Protein Modifications, Post-Translational
D005786 Gene Expression Regulation Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control (induction or repression) of gene action at the level of transcription or translation. Gene Action Regulation,Regulation of Gene Expression,Expression Regulation, Gene,Regulation, Gene Action,Regulation, Gene Expression
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000072417 Protein Domains Discrete protein structural units that may fold independently of the rest of the protein and have their own functions. Peptide Domain,Protein Domain,Domain, Peptide,Domain, Protein,Domains, Peptide,Domains, Protein,Peptide Domains
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D020033 Protein Isoforms Different forms of a protein that may be produced from different GENES, or from the same gene by ALTERNATIVE SPLICING. Isoform,Isoforms,Protein Isoform,Protein Splice Variant,Splice Variants, Protein,Protein Splice Variants,Isoform, Protein,Isoforms, Protein,Splice Variant, Protein,Variant, Protein Splice,Variants, Protein Splice
D021381 Protein Transport The process of moving proteins from one cellular compartment (including extracellular) to another by various sorting and transport mechanisms such as gated transport, protein translocation, and vesicular transport. Cellular Protein Targeting,Gated Protein Transport,Protein Targeting, Cellular,Protein Translocation,Transmembrane Protein Transport,Vesicular Protein Transport,Protein Localization Processes, Cellular,Protein Sorting,Protein Trafficking,Protein Transport, Gated,Protein Transport, Transmembrane,Protein Transport, Vesicular,Traffickings, Protein
D025542 Neurofibromin 1 A protein found most abundantly in the nervous system. Defects or deficiencies in this protein are associated with NEUROFIBROMATOSIS 1, Watson syndrome, and LEOPARD syndrome. Mutations in the gene (GENE, NEUROFIBROMATOSIS 1) affect two known functions: regulation of ras-GTPase and tumor suppression. Neurofibromatosis Type 1 Protein,NF-1 Protein,NF1 GRP,NF1 Protein,NF1-GAP-Related Protein,Neurofibromatosis Type 1 Gene Product,Neurofibromin,NF 1 Protein,NF1 GAP Related Protein

Related Publications

Mohammed Bergoug, and Michel Doudeau, and Fabienne Godin, and Christine Mosrin, and Béatrice Vallée, and Hélène Bénédetti
[Neurofibromin - protein structure and cellular functions in the context of neurofibromatosis type I pathogenesis].
December 2015, Postepy higieny i medycyny doswiadczalnej (Online),
Mohammed Bergoug, and Michel Doudeau, and Fabienne Godin, and Christine Mosrin, and Béatrice Vallée, and Hélène Bénédetti
Prostate gland: structure, functions and regulation.
January 1995, International urology and nephrology,
Mohammed Bergoug, and Michel Doudeau, and Fabienne Godin, and Christine Mosrin, and Béatrice Vallée, and Hélène Bénédetti
Rap2B GTPase: structure, functions, and regulation.
June 2016, Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine,
Mohammed Bergoug, and Michel Doudeau, and Fabienne Godin, and Christine Mosrin, and Béatrice Vallée, and Hélène Bénédetti
Telomerase: structure, functions, and activity regulation.
December 2010, Biochemistry. Biokhimiia,
Mohammed Bergoug, and Michel Doudeau, and Fabienne Godin, and Christine Mosrin, and Béatrice Vallée, and Hélène Bénédetti
Neddylation regulation of mitochondrial structure and functions.
March 2021, Cell & bioscience,
Mohammed Bergoug, and Michel Doudeau, and Fabienne Godin, and Christine Mosrin, and Béatrice Vallée, and Hélène Bénédetti
P21 activated kinases: structure, regulation, and functions.
January 2014, Small GTPases,
Mohammed Bergoug, and Michel Doudeau, and Fabienne Godin, and Christine Mosrin, and Béatrice Vallée, and Hélène Bénédetti
ACP5: Its Structure, Distribution, Regulation and Novel Functions.
January 2018, Anti-cancer agents in medicinal chemistry,
Mohammed Bergoug, and Michel Doudeau, and Fabienne Godin, and Christine Mosrin, and Béatrice Vallée, and Hélène Bénédetti
[Calcineurin: structure and regulation of the cellular functions].
September 1998, Tanpakushitsu kakusan koso. Protein, nucleic acid, enzyme,
Mohammed Bergoug, and Michel Doudeau, and Fabienne Godin, and Christine Mosrin, and Béatrice Vallée, and Hélène Bénédetti
PinX1: structure, regulation and its functions in cancer.
October 2016, Oncotarget,
Mohammed Bergoug, and Michel Doudeau, and Fabienne Godin, and Christine Mosrin, and Béatrice Vallée, and Hélène Bénédetti
Neurofibromin regulation of ERK signaling modulates GABA release and learning.
October 2008, Cell,
Copied contents to your clipboard!