gopubmed logo
find other proteinsAll proteins
GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

Atlastin GTPase 2

WWP2, ATL-2, AIP2, Dld2p
This gene encodes a member of the NEDD4-like protein family. The family of proteins is known to possess ubiquitin-protein ligase activity. The encoded protein contains 4 tandem WW domains. The WW domain is a protein motif consisting of 35 to 40 amino acids and is characterized by 4 conserved aromatic residues. The WW domain may mediate specific protein-protein interactions. Three alternatively spliced transcript variants encoding distinct isoforms have been found for this gene. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: Ubiquitin, Nedd4, V1a, CAN, ACID
Papers on WWP2
Inhibition of WWP2 suppresses proliferation, and induces G1 cell cycle arrest and apoptosis in liver cancer cells.
Wang et al., Lishui, China. In Mol Med Report, Feb 2016
As numerous studies have revealed that WW domain containing E3 Ub‑protein ligase 2 (WWP2) exerts cancer‑specific functions, the present study assessed the role of WWP2 in liver cancer.
The α-arrestin ARRDC3 mediates ALIX ubiquitination and G protein-coupled receptor lysosomal sorting.
Trejo et al., San Diego, United States. In Mol Biol Cell, Jan 2016
A screen of nine mammalian NEDD4-family E3 ubiquitin ligases revealed a critical role for WWP2.
Silencing of WWP2 inhibits adhesion, invasion, and migration in liver cancer cells.
Fu et al., Lishui, China. In Tumour Biol, Jan 2016
UNASSIGNED: The role and clinical implication of the WWP2 E3 ubiquitin ligase in liver cancer are poorly understood.
Disinhibition of the HECT E3 ubiquitin ligase WWP2 by polymerized Dishevelled.
Bienz et al., Cambridge, United Kingdom. In Open Biol, Dec 2015
Here, we show that Dvl2 binds to the ubiquitin ligase WWP2 and unlocks its ligase activity from autoinhibition.
Structure of the HECT domain of human WWP2.
Li et al., Taiwan. In Acta Crystallogr Sect F Struct Biol Commun, Oct 2015
WWP2 is a HECT-domain ubiquitin ligase of the Nedd4 family, which is involved in various important biological processes, such as protein degradation, membrane-protein sorting and transportation, the immune response, pluripotency of embryonic stem cells, tumourigenesis and metastasis.
Itch WW Domains Inhibit Its E3 Ubiquitin Ligase Activity by Blocking E2-E3 Ligase Trans-thiolation.
Oliver et al., Philadelphia, United States. In J Biol Chem, Oct 2015
This molecular switch also regulates the closely related family member WWP2.
WWP2 is required for normal cell cycle progression.
Dai et al., New York City, United States. In Genes Cancer, Sep 2015
WWP2 is a ubiquitin E3 ligase belonging to the Nedd4-like family.
WWP2 and its association with PTEN in endometrial cancer.
Leone et al., United States. In Gynecol Oncol Rep, Aug 2015
We wished to determine if WWP2 gene expression and PTEN protein levels inversely correlate in human endometrial cancer tissues.
Regulation of the PI3K pathway through a p85α monomer-homodimer equilibrium.
Mills et al., Houston, United States. In Elife, 2014
As a consequence, homodimeric but not monomeric p85α suppresses the PI3K pathway by protecting PTEN from E3 ligase WWP2-mediated proteasomal degradation.
WWP2: a multifunctional ubiquitin ligase gene.
Luo et al., Nanchong, China. In Pathol Oncol Res, 2014
WWP2, a recently identified ubiquitin E3 ligase, has been proved a multifunctional gene by degradation a series of targets via ubiquitin-dependent proteasome system, including PETN, Smads, Oct4, EGR2, TIRF and so.
An intramolecular salt bridge drives the soluble domain of GTP-bound atlastin into the postfusion conformation.
Lee et al., Pittsburgh, United States. In J Cell Biol, 2011
The role of GTP hydrolysis in the ATL2 fusion mechanism also needs to be tempered by the uncertainty of whether the behavior of the ATL2 soluble domain, observed herein, reflects the behavior of the full-length, membrane-anchored protein.
Pin1 and WWP2 regulate GluR2 Q/R site RNA editing by ADAR2 with opposing effects.
O'Connell et al., Edinburgh, United Kingdom. In Embo J, 2011
ADAR2 protein levels and catalytic activity are coordinately regulated in a positive manner by Pin1 and negatively by WWP2 and this may have downstream effects on the function of glutamate receptor 2.
MiR-140 is co-expressed with Wwp2-C transcript and activated by Sox9 to target Sp1 in maintaining the chondrocyte proliferation.
Guo et al., Shanghai, China. In Febs Lett, 2011
Data show that MiR-140 is co-expressed with Wwp2-C and is activated by Sox9 to target Sp1 in maintaining chondrocyte proliferation.
Unraveling the transcriptional regulatory machinery in chondrogenesis.
Lefebvre et al., Kyoto, Japan. In J Bone Miner Metab, 2011
Sox9 possesses a potent transactivation domain and thereby recruits diverse transcriptional co-activators, histone-modifying enzymes, subunits of the mediator complex, and components of the general transcriptional machinery, such as CBP/p300, Med12, Med25, and Wwp2.
WWP2 is an E3 ubiquitin ligase for PTEN.
Chen et al., Hyderābād, India. In Nat Cell Biol, 2011
WWP2 controls cellular apoptosis and is required for tumorigenicity of cells
[Transcriptional regulation in chondrogenesis by Sox9].
Akiyama, Kyoto, Japan. In Clin Calcium, 2011
Recent studies showed that p300÷CBP, Trap230 (med12) , Wwp2, and Med25 are components of transcriptional machinery of Sox9 in chondrogenesis.
The E3 ubiquitin ligase Wwp2 regulates craniofacial development through mono-ubiquitylation of Goosecoid.
Jones et al., Boston, United States. In Nat Cell Biol, 2011
Studies demonstrate that Wwp2 influences craniofacial patterning through its interactions with Goosecoid (Gsc).
Wwp2 is essential for palatogenesis mediated by the interaction between Sox9 and mediator subunit 25.
Akiyama et al., Tokyo, Japan. In Nat Commun, 2010
The regulatory interaction between Sox9, Wwp2 and Med25 defines the Sox9 transcriptional mechanisms of chondrogenesis in the forming palate.
The role of Nedd4/Nedd4-like dependant ubiquitylation in epithelial transport processes.
Staub et al., Lausanne, Switzerland. In Pflugers Arch, 2003
The regulation of ENaC by Nedd4-2 is a paradigm for the control of epithelial membrane proteins, as evidenced by the regulation of the ClC-5 chloride channel by the ubiquitin-protein ligase WWP2 or the tight junction protein Occludin by Itch.
share on facebooktweetadd +1mail to friends