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WAS/WASL interacting protein family, member 1

WIP, WASP-interacting protein
This gene encodes a protein that plays an important role in the organization of the actin cytoskeleton. The encoded protein binds to a region of Wiskott-Aldrich syndrome protein that is frequently mutated in Wiskott-Aldrich syndrome, an X-linked recessive disorder. Impairment of the interaction between these two proteins may contribute to the disease. Two transcript variants encoding the same protein have been identified for this gene. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: Wasp, Actin, N-WASP, Arp2, Nck
Papers using WIP antibodies
Sra-1 and Nap1 link Rac to actin assembly driving lamellipodia formation.
Chisholm Andrew D., In PLoS Genetics, 2003
... The antibodies used were: monoclonal anti-CIP4 (BD Transduction Laboratories), anti-Vinculin (Sigma), anti-WIP (Santa Cruz Biotechnology) and monoclonal anti-ABI-1 ...
Papers on WIP
Invadopodia proteins, cortactin, N-WASP and WIP differentially promote local invasiveness in ameloblastoma.
Ng et al., Kuala Lumpur, Malaysia. In J Oral Pathol Med, Feb 2016
Other invadopodia regulators, namely N-WASP, WIP and Src kinase remain unclarified.
Expression profiles of sugarcane under drought conditions: Variation in gene regulation.
Almeida et al., Arapiraca, Brazil. In Genet Mol Biol, Dec 2015
Total RNA was extracted from leaves and the expression of SAMDC, ZmPIP2-1 protein, ZmTIP4-2 protein, WIP protein, LTP protein, histone H3, DNAj, ferredoxin I, β-tubulin, photosystem I, gene 1 and gene 2 was analyzed by quantitative real-time PCR (RT-PCR).
An Engineered Minimal WASP-Myosin Fusion Protein Reveals Essential Functions for Endocytosis.
Drubin et al., Berkeley, United States. In Dev Cell, Dec 2015
During CME in yeast, actin polymerization is triggered and coordinated by a six-protein WASP/Myosin complex that includes WASP, class I myosins (Myo3 and Myo5), WIP (Vrp1), and two other proteins.
Neuritic complexity of hippocampal neurons depends on WIP-mediated mTORC1 and Abl family kinases activities.
Antón et al., Madrid, Spain. In Brain Behav, Nov 2015
The actin-binding molecule WIP (Wiskott-Aldrich syndrome protein [WASP]-interacting protein) was identified as a negative regulator of neuritogenesis.
Wiskott-Aldrich Syndrome Interacting Protein Deficiency Uncovers the Role of the Co-receptor CD19 as a Generic Hub for PI3 Kinase Signaling in B Cells.
Batista et al., Boston, United States. In Immunity, Nov 2015
Humans with Wiskott-Aldrich syndrome display a progressive immunological disorder associated with compromised Wiskott-Aldrich Syndrome Interacting Protein (WIP) function.
SUN anchors pollen WIP-WIT complexes at the vegetative nuclear envelope and is necessary for pollen tube targeting and fertility.
Meier et al., Columbus, United States. In J Exp Bot, Oct 2015
Plant LINC complexes have recently been identified in Arabidopsis thaliana, with the inner nuclear membrane SUN and outer nuclear membrane WIP proteins comprising the first identified complex.
The WASP-WIP complex in the molecular pathogenesis of Wiskott-Aldrich syndrome.
Sasahara, Japan. In Pediatr Int, Oct 2015
Here, I review our recent research on WASP and the WASP-interacting protein (WIP) complex in T cells.
Human Immunodeficiencies Related to Defective APC/T Cell Interaction.
Benvenuti et al., Rozzano, Italy. In Front Immunol, 2014
Present evidences suggest that other recently characterized primary immune deficiencies caused by mutation in genes linked to actin cytoskeletal reorganization, such as WIP and DOCK8, may also depend on altered synapse stability.
WIP: more than a WASp-interacting protein.
Barda-Saad et al., Ramat Gan, Israel. In J Leukoc Biol, 2014
WIP plays an important role in the remodeling of the actin cytoskeleton, which controls cellular activation, proliferation, and function.
WIP: WASP-interacting proteins at invadopodia and podosomes.
Antón et al., Madrid, Spain. In Eur J Cell Biol, 2012
WASP (Wiskott-Aldrich syndrome protein) and WIP (WASP-interacting protein) localise to the actin rich core of podosomes and play a critical role in their formation.
The enteropathogenic E. coli effector EspH promotes actin pedestal formation and elongation via WASP-interacting protein (WIP).
Frankel et al., London, United Kingdom. In Cell Microbiol, 2012
This study implicates WIP in enteropathogenic Escherichia coli-mediated actin polymerization and pedestal elongation.
WIP is a negative regulator of neuronal maturation and synaptic activity.
Anton et al., Madrid, Spain. In Cereb Cortex, 2012
These findings reveal WIP as a previously unreported regulator of neuronal maturation and synaptic activity
A novel primary human immunodeficiency due to deficiency in the WASP-interacting protein WIP.
Giliani et al., Brescia, Italy. In J Exp Med, 2012
These findings indicate that WIP deficiency should be suspected in patients with features of WAS in whom WAS sequence and mRNA levels are normal.
WIP remodeling actin behind the scenes: how WIP reshapes immune and other functions.
Barda-Saad et al., Ramat Gan, Israel. In Int J Mol Sci, 2011
WASp interacting protein (WIP) was first discovered as the binding partner of WASp, through the use of the yeast two hybrid system.
N-WASP regulates the epithelial junctional actin cytoskeleton through a non-canonical post-nucleation pathway.
Yap et al., Brisbane, Australia. In Nat Cell Biol, 2011
Indeed, the junctional impact of N-WASP was mediated by the WIP-family protein, WIRE, which binds to the N-WASP WH1 domain.
Actin-binding protein-1 interacts with WASp-interacting protein to regulate growth factor-induced dorsal ruffle formation.
Huttenlocher et al., Madison, United States. In Mol Biol Cell, 2010
These findings identify a novel role for mAbp1 in growth factor-induced dorsal ruffle formation through its interaction with WIP.
Characterization of Wiskott-Aldrich syndrome (WAS) mutants using Saccharomyces cerevisiae.
Thanabalu et al., Singapore, Singapore. In Fems Yeast Res, 2009
The results suggest that some of the mutations in the WH1 domain cause the Wiskott-Aldrich syndrome syndrome in humans by perturbing the WASP-WIP complex formation.
The rate of N-WASP exchange limits the extent of ARP2/3-complex-dependent actin-based motility.
Way et al., London, United Kingdom. In Nature, 2009
Taking advantage of this, we have analysed the dynamics of neuronal Wiskott-Aldrich syndrome protein (N-WASP), WASP-interacting protein (WIP), GRB2 and NCK, which are required to stimulate actin-related protein (ARP)2/3-complex-dependent actin-based motility of vaccinia virus, using fluorescence recovery after photobleaching.
Toca-1 mediates Cdc42-dependent actin nucleation by activating the N-WASP-WIP complex.
Kirschner et al., Boston, United States. In Cell, 2004
Toca-1 promotes actin nucleation by activating the N-WASP-WIP/CR16 complex, the predominant form of N-WASP in cells.
Structure of the N-WASP EVH1 domain-WIP complex: insight into the molecular basis of Wiskott-Aldrich Syndrome.
Lim et al., Milwaukee, United States. In Cell, 2002
show that the N-WASP EVH1 domain specifically binds a 25 residue motif from the WASP Interacting Protein (WIP)
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