(Q28206156)

English

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

scientific article (publication date: 17 September 2002)

In more languages

edit

Statements

instance of

scholarly article

0 references

title

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

0 references

Michael Way

2

0 references

author name string

Markus Zettl

series ordinal

1

0 references

language of work or name

English

0 references

publication date

17 September 2002

0 references

published in

Current Biology

0 references

volume

12

0 references

issue

18

0 references

page(s)

1617-22

0 references

cites work

A complex of N-WASP and WIP integrates signalling cascades that lead to actin polymerization

1 reference

stated in

Crossref

reference URL

https://api.crossref.org/works/10.1016%2FS0960-9822%2802%2901112-0

retrieved

7 January 2021

based on heuristic

inferred from DOI database lookup

WIP regulates N-WASP-mediated actin polymerization and filopodium formation

1 reference

stated in

Crossref

reference URL

https://api.crossref.org/works/10.1016%2FS0960-9822%2802%2901112-0

retrieved

7 January 2021

based on heuristic

inferred from DOI database lookup

Cutting edge: WIP, a binding partner for Wiskott-Aldrich syndrome protein, cooperates with Vav in the regulation of T cell activation

1 reference

stated in

Crossref

reference URL

https://api.crossref.org/works/10.1016%2FS0960-9822%2802%2901112-0

retrieved

7 January 2021

based on heuristic

inferred from DOI database lookup

WIP deficiency reveals a differential role for WIP and the actin cytoskeleton in T and B cell activation

1 reference

stated in

Crossref

reference URL

https://api.crossref.org/works/10.1016%2FS0960-9822%2802%2901112-0

retrieved

7 January 2021

based on heuristic

inferred from DOI database lookup

WIP, a protein associated with wiskott-aldrich syndrome protein, induces actin polymerization and redistribution in lymphoid cells

1 reference

stated in

Crossref

reference URL

https://api.crossref.org/works/10.1016%2FS0960-9822%2802%2901112-0

retrieved

7 January 2021

based on heuristic

inferred from DOI database lookup

Structure of EVH1, a novel proline-rich ligand-binding module involved in cytoskeletal dynamics and neural function

1 reference

stated in

Crossref

reference URL

https://api.crossref.org/works/10.1016%2FS0960-9822%2802%2901112-0

retrieved

7 January 2021

based on heuristic

inferred from DOI database lookup

Structure of the enabled/VASP homology 1 domain-peptide complex: a key component in the spatial control of actin assembly

1 reference

stated in

Crossref

reference URL

https://api.crossref.org/works/10.1016%2FS0960-9822%2802%2901112-0

retrieved

7 January 2021

based on heuristic

inferred from DOI database lookup

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

1 reference

stated in

Crossref

reference URL

https://api.crossref.org/works/10.1016%2FS0960-9822%2802%2901112-0

retrieved

7 January 2021

based on heuristic

inferred from DOI database lookup

Dual epitope recognition by the VASP EVH1 domain modulates polyproline ligand specificity and binding affinity

1 reference

stated in

Crossref

reference URL

https://api.crossref.org/works/10.1016%2FS0960-9822%2802%2901112-0

retrieved

7 January 2021

based on heuristic

inferred from DOI database lookup

Doing (F/L)PPPPs: EVH1 domains and their proline-rich partners in cell polarity and migration

1 reference

stated in

Crossref

reference URL

https://api.crossref.org/works/10.1016%2FS0960-9822%2802%2901112-0

retrieved

7 January 2021

based on heuristic

inferred from DOI database lookup

EVH1/WH1 domains of VASP and WASP proteins belong to a large family including Ran-binding domains of the RanBP1 family

1 reference

stated in

Crossref

reference URL

https://api.crossref.org/works/10.1016%2FS0960-9822%2802%2901112-0

retrieved

7 January 2021

based on heuristic

inferred from DOI database lookup

CR16 forms a complex with N-WASP in brain and is a novel member of a conserved proline-rich actin-binding protein family

1 reference

stated in

Crossref

reference URL

https://api.crossref.org/works/10.1016%2FS0960-9822%2802%2901112-0

retrieved

7 January 2021

based on heuristic

inferred from DOI database lookup

WICH, a novel verprolin homology domain-containing protein that functions cooperatively with N-WASP in actin-microspike formation

1 reference

stated in

Crossref

reference URL

https://api.crossref.org/works/10.1016%2FS0960-9822%2802%2901112-0

retrieved

7 January 2021

based on heuristic

inferred from DOI database lookup

The WASp homologue Las17p functions with the WIP homologue End5p/verprolin and is essential for endocytosis in yeast

1 reference

stated in

Crossref

reference URL

https://api.crossref.org/works/10.1016%2FS0960-9822%2802%2901112-0

retrieved

7 January 2021

based on heuristic

inferred from DOI database lookup

The Saccharomyces cerevisiae homologue of human Wiskott-Aldrich syndrome protein Las17p interacts with the Arp2/3 complex.

1 reference

stated in

Crossref

reference URL

https://api.crossref.org/works/10.1016%2FS0960-9822%2802%2901112-0

retrieved

7 January 2021

based on heuristic

inferred from DOI database lookup

A role for myosin-I in actin assembly through interactions with Vrp1p, Bee1p, and the Arp2/3 complex

1 reference

stated in

Crossref

reference URL

https://api.crossref.org/works/10.1016%2FS0960-9822%2802%2901112-0

retrieved

7 January 2021

based on heuristic

inferred from DOI database lookup

N-WASP deficiency reveals distinct pathways for cell surface projections and microbial actin-based motility

1 reference

stated in

Crossref

reference URL

https://api.crossref.org/works/10.1016%2FS0960-9822%2802%2901112-0

retrieved

7 January 2021

based on heuristic

inferred from DOI database lookup

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

1 reference

stated in

Crossref

reference URL

https://api.crossref.org/works/10.1016%2FS0960-9822%2802%2901112-0

retrieved

7 January 2021

based on heuristic

inferred from DOI database lookup

Identifiers

DOI

10.1016/S0960-9822(02)01112-0

0 references

PubMed publication ID

12372256

0 references

ResearchGate publication ID

11088056

0 references

(Q28206156)

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

Statements

Identifiers

Sitelinks

Wikipedia(0 entries)

Wikibooks(0 entries)

Wikinews(0 entries)

Wikiquote(0 entries)

Wikisource(0 entries)

Wikiversity(0 entries)

Wikivoyage(0 entries)

Wiktionary(0 entries)

Multilingual sites(0 entries)