A BAR domain in the N terminus of the Arf GAP ASAP1 affects membrane structure and trafficking of epidermal growth factor receptor.
about
Amphipathic motifs in BAR domains are essential for membrane curvature sensingMolecular complexes that direct rhodopsin transport to primary ciliaStructure of Rab11-FIP3-Rabin8 reveals simultaneous binding of FIP3 and Rabin8 effectors to Rab11Arf GTPase-activating protein ASAP1 interacts with Rab11 effector FIP3 and regulates pericentrosomal localization of transferrin receptor-positive recycling endosomeAutoinhibition of Arf GTPase-activating protein activity by the BAR domain in ASAP1Ciliary targeting motif VxPx directs assembly of a trafficking module through Arf4.A conserved signal and GTPase complex are required for the ciliary transport of polycystin-1.The Arf GAP ASAP1 provides a platform to regulate Arf4- and Rab11-Rab8-mediated ciliary receptor targeting.Crosstalk of Arf and Rab GTPases en route to cilia.ACAP-A/B are ArfGAP homologs in dictyostelium involved in sporulation but not in chemotaxisThe Arf and Rab11 effector FIP3 acts synergistically with ASAP1 to direct Rabin8 in ciliary receptor targetingSrc-dependent phosphorylation of ASAP1 regulates podosomes.Force-control at cellular membranesThe RabGAP proteins Gyp5p and Gyl1p recruit the BAR domain protein Rvs167p for polarized exocytosis.ASAP1 promotes tumor cell motility and invasiveness, stimulates metastasis formation in vivo, and correlates with poor survival in colorectal cancer patients.Kinetic analysis of GTP hydrolysis catalysed by the Arf1-GTP-ASAP1 complexCharacterization of recombinant ELMOD (cell engulfment and motility domain) proteins as GTPase-activating proteins (GAPs) for ARF family GTPases.Membrane targeting by APPL1 and APPL2: dynamic scaffolds that oligomerize and bind phosphoinositides.Arf GAPs: gatekeepers of vesicle generation.Ciliopathies: the trafficking connection.ARAP1 regulates endocytosis of EGFR.Models for the functions of Arf GAPs.ArfGAP1 promotes COPI vesicle formation by facilitating coatomer polymerizationGTP-binding protein-like domain of AGAP1 is protein binding site that allosterically regulates ArfGAP protein catalytic activity.Molecular Basis for Cooperative Binding of Anionic Phospholipids to the PH Domain of the Arf GAP ASAP1.Kinetic analysis of Arf GAP1 indicates a regulatory role for coatomer.Arf GAPs and their interacting proteins.Arf GAPs as regulators of the actin cytoskeleton.Dynamic interaction between Arf GAP and PH domains of ASAP1 in the regulation of GAP activityArf GTPase-activating proteins and their potential role in cell migration and invasionProtein sorting, targeting and trafficking in photoreceptor cellsArf GAP2 is positively regulated by coatomer and cargo.The EGFR-GEP100-Arf6-AMAP1 signaling pathway specific to breast cancer invasion and metastasis.Modeling membrane deformations and lipid demixing upon protein-membrane interaction: the BAR dimer adsorption.Overexpression of ASAP1 is associated with poor prognosis in epithelial ovarian cancer.A PH domain in the Arf GTPase-activating protein (GAP) ARAP1 binds phosphatidylinositol 3,4,5-trisphosphate and regulates Arf GAP activity independently of recruitment to the plasma membranes.The Arf GAP AGAP2 interacts with β-arrestin2 and regulates β2-adrenergic receptor recycling and ERK activation.eIF5B increases ASAP1 expression to promote HCC proliferation and invasion.Molecular mechanisms of protein and lipid targeting to ciliary membranes.COPII and COPI traffic at the ER-Golgi interface.
P2860
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P2860
A BAR domain in the N terminus of the Arf GAP ASAP1 affects membrane structure and trafficking of epidermal growth factor receptor.
description
2006 nî lūn-bûn
@nan
2006 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2006 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
name
A BAR domain in the N terminus ...... dermal growth factor receptor.
@ast
A BAR domain in the N terminus ...... dermal growth factor receptor.
@en
A BAR domain in the N terminus ...... dermal growth factor receptor.
@nl
type
label
A BAR domain in the N terminus ...... dermal growth factor receptor.
@ast
A BAR domain in the N terminus ...... dermal growth factor receptor.
@en
A BAR domain in the N terminus ...... dermal growth factor receptor.
@nl
altLabel
A BAR domain in the N terminus ...... idermal growth factor receptor
@en
prefLabel
A BAR domain in the N terminus ...... dermal growth factor receptor.
@ast
A BAR domain in the N terminus ...... dermal growth factor receptor.
@en
A BAR domain in the N terminus ...... dermal growth factor receptor.
@nl
P2093
P1433
P1476
A BAR domain in the N terminus ...... dermal growth factor receptor.
@en
P2093
Aida Cremesti
Bijan Ahvazi
Dianne S Hirsch
Jacob Lebowitz
Jenny E Hinshaw
Josefa Andrade
Michael Marino
Paul A Randazzo
Ruibai Luo
Stacey Stauffer
P356
10.1016/J.CUB.2005.11.069
P407
P577
2006-01-24T00:00:00Z