The WH1 and EVH1 domains of WASP and Ena/VASP family members bind distinct sequence motifs

Current Biology

Volumn 12, Issue 18, 2002, Pages 1617-1622

  Zettl, Markus ^a   Way, Michael ^a  

^a THE FRANCIS CRICK INSTITUTE   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; CARRIER PROTEIN; DNA BINDING PROTEIN; ENA/VASP PROTEINS; NERVE PROTEIN; NEURAL WISKOTT ALDRICH SYNDROME PROTEIN; PROTEIN; RECOMBINANT PROTEIN; SACCHAROMYCES CEREVISIAE PROTEIN; SCHIZOSACCHAROMYCES POMBE PROTEIN; WAS PROTEIN, HUMAN; WASL PROTEIN, HUMAN; WASPIP PROTEIN, HUMAN; WISKOTT ALDRICH SYNDROME PROTEIN;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; CHEMISTRY; GENETICS; HUMAN; IN VITRO STUDY; METABOLISM; MOLECULAR GENETICS; NUCLEOTIDE SEQUENCE; PROTEIN BINDING; PROTEIN MOTIF; PROTEIN TERTIARY STRUCTURE; SHIGELLA; SITE DIRECTED MUTAGENESIS; VACCINIA VIRUS;

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; BACTERIAL PROTEINS; CARRIER PROTEINS; CONSERVED SEQUENCE; DNA-BINDING PROTEINS; HUMANS; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; NERVE TISSUE PROTEINS; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; PROTEINS; RECOMBINANT PROTEINS; SACCHAROMYCES CEREVISIAE PROTEINS; SCHIZOSACCHAROMYCES POMBE PROTEINS; SHIGELLA; VACCINIA VIRUS; WISKOTT-ALDRICH SYNDROME PROTEIN; WISKOTT-ALDRICH SYNDROME PROTEIN, NEURONAL;

BACTERIA (MICROORGANISMS); ENA; SACCHAROMYCES; SACCHAROMYCES CEREVISIAE; SCHIZOSACCHAROMYCES; SCHIZOSACCHAROMYCES POMBE; SHIGELLA; VACCINIA VIRUS;

EID: 0037125912     PISSN: 09609822     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0960-9822(02)01112-0     Document Type: Article

References (19)

1. A complex of N-WASP and WIP integrates signalling cascades that lead to actin polymerization
2. WIP regulates N-WASP-mediated actin polymerization and filopodium formation
3. Cutting edge: WIP, a binding partner for Wiskott-Aldrich syndrome protein, cooperates with Vav in the regulation of T cell activation
4. WIP deficiency reveals a differential role for WIP and the actin cytoskeleton in T and B cell activation
5. WIP, a protein associated with Wiskott-Aldrich syndrome protein, induces actin polymerization and redistribution in lymphoid cells
6. Mutations that cause Wiskott-Aldrich syndrome impair the interaction of Wiskott-Aldrich syndrome protein (WASP) with WASP interacting protein
7. Structure of EVH1, a novel proline-rich ligand-binding module involved in cytoskeletal dynamics and neural function
8. Structure of the Enabled/VASP homology 1 domain-peptide complex: A key component in the spatial control of actin assembly
9. A novel proline-rich motif present in ActA of Listeria monocytogenes and cytoskeletal proteins is the ligand for the EVH1 domain, a protein module present in the Ena/VASP family
10. Dual epitope recognition by the VASP EVH1 domain modulates polyproline ligand specificity and binding affinity
11. Doing (F/L)PPPPs: EVH1 domains and their proline-rich partners in cell polarity and migration
12. EVH1/WH1 domains of VASP and WASP proteins belong to a large family including Ran-binding domains of the RanBP1 family
13. CR16 forms a complex with N-WASP in brain and is a novel member of a conserved proline-rich actin-binding protein family
14. WICH, a novel verprolin homology domain-containing protein that functions cooperatively with N-WASP in actin-microspike formation
15. The WASp homologue Las17p functions with the Wlp homologue End5p/verprolin and is essential for endocytosis
16. The Saccharomyces cerevisiae homologue of human Wiskott-Aldrich syndrome protein Las17p interacts with the Arp2/3 complex
17. A role for myosin-I in actin assembly through interactions with Vrp1p, Bee1p and the Arp2/3 complex
18. N-WASP deficiency reveals distinct pathways for cell surface projections and microbial actin-based motility
19. The rat homologue of Wiskott-Aldrich syndrome protein (WASP)-interacting protein (WIP) associates with actin filaments, recruits N-WASP from the nucleus, and mediates mobilization of actin from stress fibers in favor of filopodia formation