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

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

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

http://www.wikidata.org/entity/Q27939506

about

The BAR domain proteins: molding membranes in fission, fusion, and phagy The yeast actin cytoskeleton: from cellular function to biochemical mechanism Direct regulation of Arp2/3 complex activity and function by the actin binding protein coronin Actin, Membrane Trafficking and the Control of Prion Induction, Propagation and Transmission in Yeast Clathrin-mediated endocytosis in budding yeast Lsb1 is a negative regulator of las17 dependent actin polymerization involved in endocytosis Identification of an ATP-controlled allosteric switch that controls actin filament nucleation by Arp2/3 complex.Movement of yeast 1,3-beta-glucan synthase is essential for uniform cell wall synthesis.Saccharomyces cerevisiae contains a Type II phosphoinositide 4-kinase Lsb5p interacts with actin regulators Sla1p and Las17p, ubiquitin and Arf3p to couple actin dynamics to membrane trafficking processes Sla1p serves as the targeting signal recognition factor for NPFX(1,2)D-mediated endocytosis.A network of proteins around Rvs167p and Rvs161p, two proteins related to the yeast actin cytoskeleton.Saccharomyces cerevisiae Bzz1p is implicated with type I myosins in actin patch polarization and is able to recruit actin-polymerizing machinery in vitro Rvs161p and Rvs167p, the two yeast amphiphysin homologs, function together in vivo.A novel link between a rab GTPase and Rvs proteins: the yeast amphiphysin homologues.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 Scd5p and clathrin function are important for cortical actin organization, endocytosis, and localization of sla2p in yeast.A protein interaction map for cell polarity development.Dynamic organization of the actin cytoskeleton during meiosis and spore formation in budding yeast.A novel single-cell screening platform reveals proteome plasticity during yeast stress responses Novel proteins linking the actin cytoskeleton to the endocytic machinery in Saccharomyces cerevisiae Effects of Arp2 and Arp3 nucleotide-binding pocket mutations on Arp2/3 complex function.Regulation of the yeast amphiphysin homologue Rvs167p by phosphorylation.The Rsp5 ubiquitin ligase binds to and ubiquitinates members of the yeast CIN85-endophilin complex, Sla1-Rvs167.The WASP homologue Las17 activates the novel actin-regulatory activity of Ysc84 to promote endocytosis in yeast Rho1p and Cdc42p act after Ypt7p to regulate vacuole docking.Yeast Arf3p modulates plasma membrane PtdIns(4,5)P2 levels to facilitate endocytosis.Verprolin cytokinesis function mediated by the Hof one trap domain.Vrp1p functions in both actomyosin ring-dependent and Hof1p-dependent pathways of cytokinesis.The Saccharomyces cerevisiae LSB6 gene encodes phosphatidylinositol 4-kinase activity.The WASP/Las17p-interacting protein Bzz1p functions with Myo5p in an early stage of endocytosis.The F-BAR protein Syp1 negatively regulates WASp-Arp2/3 complex activity during endocytic patch formation.Evidence for the genetic interaction between the actin-binding protein Vrp1 and the RhoGAP Rgd1 mediated through Rho3p and Rho4p in Saccharomyces cerevisiae.Existence of a novel clathrin-independent endocytic pathway in yeast that depends on Rho1 and formin.Defects in structural integrity of ergosterol and the Cdc50p-Drs2p putative phospholipid translocase cause accumulation of endocytic membranes, onto which actin patches are assembled in yeast.Membrane trafficking in the yeast Saccharomyces cerevisiae model Evolution of the SH3 Domain Specificity Landscape in Yeasts.Targeting and functional mechanisms of the cytokinesis-related F-BAR protein Hof1 during the cell cycle Functional characterization of myosin I tail regions in Candida albicans An intact SH3 domain is required for myosin I-induced actin polymerization.

P2860

5cf455746a3134187016e97624608a46f598aaf9 7be6aed7f4b4c606953825490d18959c149cbcd6 af256353885a507ca5d1a67016ceb70d27c4133c cfb089d13020d8cf8f205e6f4b09e7ec20db00ca

P248

Q24544126-845869D8-2D25-4C5A-B554-EC6010670DFE Q24669945-E52867CC-D702-4A55-BE26-8B7FF6DCA0EA Q24671425-A704696E-11A1-4580-A8C1-58ACE2F79C00 Q26778771-CCECBBAA-DF33-4443-A2BA-659EDC7E5A96 Q27022657-D4101B27-F844-412F-8E88-7AC141FD7BDB Q27325785-8ACBAD59-C266-4017-8813-4DE15470484D Q27335176-DBA2F1C3-5D8C-4271-BB57-B4CBD3EDDAAA Q27929821-E8A93557-28EC-45D2-B6C9-C87F66B4F126 Q27929859-165B96D4-E2C2-4191-9823-17939320963B Q27929982-5ECE5B01-AFF0-4877-BA7D-FAA7AF6CEAE7 Q27930516-064DF7E9-268D-47AB-A85A-E1AD2F28B73D Q27930938-6223E85D-4AE8-4E4C-A4BA-9C3446E0CDB1 Q27931652-248775AB-E734-4CF4-9E94-84ABF5DF5CDD Q27931705-458BCE2C-9E2D-4322-9E43-99E7065E7C71 Q27933712-A18C40E6-8BB3-4FD9-B313-A123E31AC06D Q27934485-E32F202B-BDF2-4AC1-8A47-F647F81714A0 Q27934772-822206E3-6700-4A7E-9E66-C3D8819022E3 Q27934870-86993DB2-DBF6-43A2-BA22-CB0EDF697717 Q27934926-FB53F78B-1A54-4BB3-ACA1-35942CF37728 Q27935802-096316D7-20C1-4681-8D94-8E758C549370 Q27936195-5D4B7821-37B6-4330-8861-EEB4C39DBB52 Q27936467-368E39B8-27EF-4649-9582-FBFEEB122703 Q27936496-0066893B-2C80-408F-93CA-6358F3B39ADD Q27936682-F4ACC7BE-2B2C-4399-8292-299488E1AB81 Q27936845-D4FDBBC7-2F94-4698-A5E0-D5496669FF1B Q27936915-4FE4AA2D-6975-43B9-AFB0-1B16ADA18F36 Q27936945-8037A709-ADE9-4DD4-AD7A-CE9BEC18C41B Q27937277-9D781351-BBE8-408D-B985-E3348763327A Q27937606-F8B45D18-BFAC-4762-B1AE-683B638BC455 Q27938509-02035F0E-C8E9-468E-B1C4-0D2590E28C71 Q27938721-C51397BD-3B2E-485C-8971-F9CFB5CFFCC6 Q27939064-FC7273EA-E037-49B1-A4BA-F360F922D421 Q27939543-EB9C4726-C2B5-46DA-9D10-C2A9A2DAFB53 Q27939804-5D3C3BCC-0952-4C43-BDC9-C58AD6B4D78B Q27940028-FAB917BF-1713-4D76-9115-71735F015485 Q28084192-068C4E41-7DAA-4352-A170-0081B4461A75 Q30009154-0CB05A6D-4497-41A0-A6A4-B6BE18D611DA Q30009904-9B39E44C-D0C4-4679-97D6-E3FF57CB8294 Q30163789-17D81B5F-E0DB-44F3-909E-38FE3B1E8456 Q30168825-B35B8002-4D58-43A3-BE43-6B76C6FA6642

P2860

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

http://www.wikidata.org/entity/Q27939506

description

1999 nî lūn-bûn

@nan

1999 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

@hyw

1999 թվականի հոտեմբերին հրատարակված գիտական հոդված

@hy

1999年の論文

@ja

1999年論文

@yue

1999年論文

@zh-hant

1999年論文

@zh-hk

1999年論文

@zh-mo

1999年論文

@zh-tw

1999年论文

@wuu

name

The Saccharomyces cerevisiae h ...... racts with the Arp2/3 complex.

@ast

The Saccharomyces cerevisiae h ...... racts with the Arp2/3 complex.

@en

The Saccharomyces cerevisiae h ...... racts with the Arp2/3 complex.

@nl

type

label

The Saccharomyces cerevisiae h ...... racts with the Arp2/3 complex.

@ast

The Saccharomyces cerevisiae h ...... racts with the Arp2/3 complex.

@en

The Saccharomyces cerevisiae h ...... racts with the Arp2/3 complex.

@nl

prefLabel

The Saccharomyces cerevisiae h ...... racts with the Arp2/3 complex.

@ast

The Saccharomyces cerevisiae h ...... racts with the Arp2/3 complex.

@en

The Saccharomyces cerevisiae h ...... racts with the Arp2/3 complex.

@nl

P1433

Q27939506-CB476E12-443B-4E2E-8A6E-EC756EABA863

P1476

Q27939506-3E259F97-BCB1-4FED-82BA-CA0513729F29

P2093

Q27939506-01EBDED9-4ACB-4A09-B3DE-3FBBBA01DF2B

Q27939506-0BB29FFC-A142-46F4-92A9-E3637CB404AA

Q27939506-5AC87B3F-86A1-4A27-8943-7941E5DDD7FA

Q27939506-6F099FD1-9A71-4B30-9457-B5781D1AC3FF

Q27939506-7828F0F9-503C-44B0-A8BF-C9CAF0099D01

Q27939506-DC3BA8B1-7BA1-47F4-B5B4-5553CF4004AC

P2860

Q27939506-02ED7A2A-1352-4B67-9B43-DA58F6F91A91

Q27939506-0803FF2E-B789-470A-8D35-36C2AAA20AB8

Q27939506-0A61B316-D400-40EE-82A9-E58CA2FB9667

Q27939506-0DE2909E-E2B9-4B67-9EBA-FAE55ED7901C

Q27939506-0E130C8D-FB4D-41EC-BF4C-4F9CFEF45B09

Q27939506-113F2C03-5484-4470-A7A3-E5D7EAA7667D

Q27939506-14972908-8BCC-4CB4-AE10-F0CB6E6684D9

Q27939506-176C951D-71A1-4F5B-9CAD-7C454124DDE8

Q27939506-1EB1E54D-CA89-413A-B8E3-A73F851977A8

Q27939506-210C744B-C60D-4D58-BC0A-41533472D1B5

P304

Q27939506-DE8B57AF-0FCE-4232-8851-0FE1941910A8

P31

Q27939506-B5F0F165-D779-42BA-8306-91D1B144C7A2

P3181

Q27939506-45D648AF-C8B6-44BB-AB6B-ECD4345C75B7

P356

Q27939506-912FB7CB-0AB8-433F-8643-DA9396CC2816

P407

Q27939506-10A2B646-A6A7-404C-8E2A-D8DC15306755

P433

Q27939506-C4BD0831-4585-4021-AA1D-88C6F905657D

P478

Q27939506-2FE0284E-60CC-485B-9659-77BEADDD2FDE

P50

Q27939506-35857B29-3EA6-4063-AAE9-D03E52B1091E

Q27939506-60B71DBB-6D09-4628-83C8-F8BF8C017D4F

P577

Q27939506-4AC2EE18-270F-4B79-8DA9-1AC39FA0C12A

P5875

Q27939506-79B7D3EA-9428-4706-A0B8-29755A5D0DCD

P698

Q27939506-72BE1D13-571E-47FF-846C-ECBF61644823

P921

Q27939506-2AAE332F-37A4-45C5-9BC1-22D6617B4D9B

Q27939506-43AA8E19-04CC-48EE-A755-482C6460F640

P932

Q27939506-3BF1DD43-5C6B-46AC-99D9-3659DAE770E9

P3181

P356

P1433

Molecular Biology of the Cell

P1476

The Saccharomyces cerevisiae h ...... eracts with the Arp2/3 complex

@en

P2093

A Madania

http://www.w3.org/2001/XMLSchema#string

B Winsor

http://www.w3.org/2001/XMLSchema#string

C Schärer-Brodbeck

http://www.w3.org/2001/XMLSchema#string

H Kitamoto

http://www.w3.org/2001/XMLSchema#string

P Dumoulin

http://www.w3.org/2001/XMLSchema#string

S Grava

http://www.w3.org/2001/XMLSchema#string

P2860

WAVE, a novel WASP-family protein involved in actin reorganization induced by Rac

Wiskott-Aldrich syndrome protein, a novel effector for the GTPase CDC42Hs, is implicated in actin polymerization

Fission yeast Sop2p: a novel and evolutionarily conserved protein that interacts with Arp3p and modulates profilin function

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

The human Arp2/3 complex is composed of evolutionarily conserved subunits and is localized to cellular regions of dynamic actin filament assembly

Direct interaction of the Wiskott-Aldrich syndrome protein with the GTPase Cdc42

The Arp2/3 complex mediates actin polymerization induced by the small GTP-binding protein Cdc42

The interaction of Arp2/3 complex with actin: nucleation, high affinity pointed end capping, and formation of branching networks of filaments

Purification of a cortical complex containing two unconventional actins from Acanthamoeba by affinity chromatography on profilin-agarose

A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae

P304

3521-3538

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P3181

4538600

http://www.w3.org/2001/XMLSchema#string

P356

10.1091/MBC.10.10.3521

http://www.w3.org/2001/XMLSchema#string

P407

P433

10

http://www.w3.org/2001/XMLSchema#string

P478

10

http://www.w3.org/2001/XMLSchema#string

P50

Violaine Moreau

P577

1999-10-01T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

12787367

http://www.w3.org/2001/XMLSchema#string

P698

10512884

http://www.w3.org/2001/XMLSchema#string

P921

Saccharomyces cerevisiae

Wiskott-Aldrich syndrome

P932

25621

http://www.w3.org/2001/XMLSchema#string