The Grb2/PLD2 interaction is essential for lipase activity, intracellular localization and signaling in response to EGF
about
A novel phospholipase D2-Grb2-WASp heterotrimer regulates leukocyte phagocytosis in a two-step mechanismA comprehensive model that explains the regulation of phospholipase D2 activity by phosphorylation-dephosphorylation.Phosphatidic acid is a leukocyte chemoattractant that acts through S6 kinase signalingPhospholipase D in cell signaling: from a myriad of cell functions to cancer growth and metastasis.The molecular basis of phospholipase D2-induced chemotaxis: elucidation of differential pathways in macrophages and fibroblasts.α-Synuclein expression in rat substantia nigra suppresses phospholipase D2 toxicity and nigral neurodegeneration.Cortactin: a multifunctional regulator of cellular invasivenessThe exquisite regulation of PLD2 by a wealth of interacting proteins: S6K, Grb2, Sos, WASp and Rac2 (and a surprise discovery: PLD2 is a GEF).Phospholipase D: enzymology, functionality, and chemical modulationPhosphatidic Acid Increases Epidermal Growth Factor Receptor Expression by Stabilizing mRNA Decay and by Inhibiting Lysosomal and Proteasomal Degradation of the Internalized ReceptorImpact of Hybrid and Complex N-Glycans on Cell Surface Targeting of the Endogenous Chloride Cotransporter Slc12a2.Biochemical and cellular implications of a dual lipase-GEF function of phospholipase D2 (PLD2).Phosphatidic Acid (PA) can Displace PPARα/LXRα Binding to The EGFR Promoter Causing its Transrepression in Luminal Cancer CellsIdentification of the catalytic site of phospholipase D2 (PLD2) newly described guanine nucleotide exchange factor activityMutation of Y179 on phospholipase D2 (PLD2) upregulates DNA synthesis in a PI3K-and Akt-dependent manner.Insights into the PX (phox-homology) domain and SNX (sorting nexin) protein families: structures, functions and roles in disease.Crosstalk of small GTPases at the Golgi apparatus.The inhibition of tube formation in a collagen-fibrinogen, three-dimensional gel by cleaved kininogen (HKa) and HK domain 5 (D5) is dependent on Src family kinases.
P2860
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P2860
The Grb2/PLD2 interaction is essential for lipase activity, intracellular localization and signaling in response to EGF
description
2007 nî lūn-bûn
@nan
2007 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2007 թվականի մարտին հրատարակված գիտական հոդված
@hy
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
name
The Grb2/PLD2 interaction is e ...... d signaling in response to EGF
@ast
The Grb2/PLD2 interaction is e ...... d signaling in response to EGF
@en
The Grb2/PLD2 interaction is e ...... d signaling in response to EGF
@en-gb
The Grb2/PLD2 interaction is e ...... d signaling in response to EGF
@nl
type
label
The Grb2/PLD2 interaction is e ...... d signaling in response to EGF
@ast
The Grb2/PLD2 interaction is e ...... d signaling in response to EGF
@en
The Grb2/PLD2 interaction is e ...... d signaling in response to EGF
@en-gb
The Grb2/PLD2 interaction is e ...... d signaling in response to EGF
@nl
prefLabel
The Grb2/PLD2 interaction is e ...... d signaling in response to EGF
@ast
The Grb2/PLD2 interaction is e ...... d signaling in response to EGF
@en
The Grb2/PLD2 interaction is e ...... d signaling in response to EGF
@en-gb
The Grb2/PLD2 interaction is e ...... d signaling in response to EGF
@nl
P2093
P2860
P1476
The Grb2/PLD2 interaction is e ...... d signaling in response to EGF
@en
P2093
Karen M Henkels
Kathleen Frondorf
Mauricio Di Fulvio
Nicholas Lehman
P2860
P304
P356
10.1016/J.JMB.2007.01.021
P407
P577
2007-01-12T00:00:00Z