scholarly journals The expression of Wiskott-Aldrich syndrome protein (WASP) is dependent on WASP-interacting protein (WIP)

2006 ◽  
Vol 19 (2) ◽  
pp. 185-192 ◽  
Author(s):  
A. Konno ◽  
M. Kirby ◽  
S. A. Anderson ◽  
P. L. Schwartzberg ◽  
F. Candotti
Keyword(s):  
Interacting Protein ◽  
Wiskott Aldrich Syndrome ◽  
Syndrome Protein

scholarly journals The Novel Adaptor Protein, Mti1p, and Vrp1p, a Homolog of Wiskott-Aldrich Syndrome Protein-Interacting Protein (WIP), May Antagonistically Regulate Type I Myosins in Saccharomyces cerevisiae

Genetics ◽  
2002 ◽  
Vol 160 (3) ◽  
pp. 923-934
Author(s):  
Junko Mochida ◽  
Takaharu Yamamoto ◽  
Konomi Fujimura-Kamada ◽  
Kazuma Tanaka
Keyword(s):  
Adaptor Protein ◽  
Actin Binding ◽  
Temperature Sensitive ◽  
Null Mutation ◽  
Type I ◽  
Cortical Actin ◽  
Tail Region ◽  
Interacting Protein ◽  
Wiskott Aldrich Syndrome ◽  
Syndrome Protein

Abstract Type I myosins in yeast, Myo3p and Myo5p (Myo3/5p), are involved in the reorganization of the actin cytoskeleton. The SH3 domain of Myo5p regulates the polymerization of actin through interactions with both Las17p, a homolog of mammalian Wiskott-Aldrich syndrome protein (WASP), and Vrp1p, a homolog of WASP-interacting protein (WIP). Vrp1p is required for both the localization of Myo5p to cortical patch-like structures and the ATP-independent interaction between the Myo5p tail region and actin filaments. We have identified and characterized a new adaptor protein, Mti1p (Myosin tail region-interacting protein), which interacts with the SH3 domains of Myo3/5p. Mti1p co-immunoprecipitated with Myo5p and Mti1p-GFP co-localized with cortical actin patches. A null mutation of MTI1 exhibited synthetic lethal phenotypes with mutations in SAC6 and SLA2, which encode actin-bundling and cortical actin-binding proteins, respectively. Although the mti1 null mutation alone did not display any obvious phenotype, it suppressed vrp1 mutation phenotypes, including temperature-sensitive growth, abnormally large cell morphology, defects in endocytosis and salt-sensitive growth. These results suggest that Mti1p and Vrp1p antagonistically regulate type I myosin functions.

scholarly journals CD44 and β3 Integrin Organize Two Functionally Distinct Actin-based Domains in Osteoclasts

2007 ◽  
Vol 18 (12) ◽  
pp. 4899-4910 ◽  
Author(s):  
Anne Chabadel ◽  
Inmaculada Bañon-Rodríguez ◽  
David Cluet ◽  
Brian B. Rudkin ◽  
Bernhard Wehrle-Haller ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Actin Cytoskeleton ◽  
Interacting Protein ◽  
Wiskott Aldrich Syndrome ◽  
Diffuse Cloud ◽  
Sealing Zone ◽  
Β3 Integrin ◽  
Syndrome Protein

The actin cytoskeleton of mature osteoclasts (OCs) adhering to nonmineralized substrates is organized in a belt of podosomes reminiscent of the sealing zone (SZ) found in bone resorbing OCs. In this study, we demonstrate that the belt is composed of two functionally different actin-based domains: podosome cores linked with CD44, which are involved in cell adhesion, and a diffuse cloud associated with β3 integrin, which is involved in cell adhesion and contraction. Wiskott Aldrich Syndrome Protein (WASp) Interacting Protein (WIP)−/− OCs were devoid of podosomes, but they still exhibited actin clouds. Indeed, WIP−/− OCs show diminished expression of WASp, which is required for podosome formation. CD44 is a novel marker of OC podosome cores and the first nonintegrin receptor detected in these structures. The importance of CD44 is revealed by showing that its clustering restores podosome cores and WASp expression in WIP−/− OCs. However, although CD44 signals are sufficient to form a SZ, the presence of WIP is indispensable for the formation of a fully functional SZ.

scholarly journals Wiskott-Aldrich syndrome protein is an effector of Kit signaling

Blood ◽  
2009 ◽  
Vol 114 (14) ◽  
pp. 2900-2908 ◽  
Author(s):  
Maheswaran Mani ◽  
Shivkumar Venkatasubrahmanyam ◽  
Mrinmoy Sanyal ◽  
Shoshana Levy ◽  
Atul Butte ◽  
...  
Keyword(s):  
Gene Expression ◽  
Positive Culture ◽  
Selective Advantage ◽  
Heterozygous Female ◽  
Interacting Protein ◽  
Wiskott Aldrich Syndrome ◽  
Underlying Mechanisms ◽  
And Migration ◽  
Induced Changes ◽  
Syndrome Protein

The pleiotropic receptor tyrosine kinase Kit can provide cytoskeletal signals that define cell shape, positioning, and migration, but the underlying mechanisms are less well understood. In this study, we provide evidence that Kit signals through Wiskott-Aldrich syndrome protein (WASP), the central hematopoietic actin nucleation-promoting factor and regulator of the cytoskeleton. Kit ligand (KL) stimulation resulted in transient tyrosine phosphorylation of WASP, as well as interacting proteins WASP-interacting protein and Arp2/3. KL-induced filopodia in bone marrow–derived mast cells (BMMCs) were significantly decreased in number and size in the absence of WASP. KL-dependent regulation of intracellular Ca2+ levels was aberrant in WASP-deficient BMMCs. When BMMCs were derived from WASP-heterozygous female mice using KL as a growth factor, the cultures eventually developed from a mixture of WASP-positive and -negative populations into a homogenous WASP-positive culture derived from the WASP-positive progenitors. Thus, WASP expression conferred a selective advantage to the development of Kit-dependent hematopoiesis consistent with the selective advantage of WASP-positive hematopoietic cells observed in WAS-heterozygous female humans. Finally, KL-mediated gene expression in wild-type and WASP-deficient BMMCs was compared and revealed that approximately 30% of all Kit-induced changes were WASP dependent. The results indicate that Kit signaling through WASP is necessary for normal Kit-mediated filopodia formation, cell survival, and gene expression, and provide new insight into the mechanism in which WASP exerts a strong selective pressure in hematopoiesis.

scholarly journals Cdc42-interacting Protein 4 Mediates Binding of the Wiskott-Aldrich Syndrome Protein to Microtubules

2000 ◽  
Vol 275 (11) ◽  
pp. 7854-7861 ◽  
Author(s):  
Lan Tian ◽  
David L. Nelson ◽  
Donn M. Stewart
Keyword(s):  
Interacting Protein ◽  
Wiskott Aldrich Syndrome ◽  
Syndrome Protein

scholarly journals The Wiskott-Aldrich Syndrome Protein-interacting Protein (WIP) Binds to the Adaptor Protein Nck

1998 ◽  
Vol 273 (33) ◽  
pp. 20992-20995 ◽  
Author(s):  
Inés M. Antón ◽  
Wange Lu ◽  
Bruce J. Mayer ◽  
Narayanaswamy Ramesh ◽  
Raif S. Geha
Keyword(s):  
Adaptor Protein ◽  
Interacting Protein ◽  
Wiskott Aldrich Syndrome ◽  
Syndrome Protein
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