Shp2 Associates with and Enhances Nephrin Tyrosine Phosphorylation and Is Necessary for Foot Process Spreading in Mouse Models of Podocyte Injury. (Q36574874)

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scientific article published on 7 December 2015

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English	Shp2 Associates with and Enhances Nephrin Tyrosine Phosphorylation and Is Necessary for Foot Process Spreading in Mouse Models of Podocyte Injury.	scientific article published on 7 December 2015

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2 March 2020

Shp2 Associates with and Enhances Nephrin Tyrosine Phosphorylation and Is Necessary for Foot Process Spreading in Mouse Models of Podocyte Injury (English)

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2 March 2020

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2 March 2020

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Rakesh Verma

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Madhusudan Venkatareddy

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Anne Kalinowski

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Sanjeevkumar R Patel

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Molecular and Cellular Biology

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596-614

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Nephrin Preserves Podocyte Viability and Glomerular Structure and Function in Adult Kidneys

1 reference

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Increased SHP-1 protein expression by high glucose levels reduces nephrin phosphorylation in podocytes

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Podocyte Protein, Nephrin, Is a Substrate of Protein Tyrosine Phosphatase 1B

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SHP2 Mediates the Localized Activation of Fyn Downstream of the α6β4 Integrin To Promote Carcinoma Invasion

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Inhibition of podocyte FAK protects against proteinuria and foot process effacement.

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30 September 2017

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30 September 2017

A conserved mechanism for control of human and mouse embryonic stem cell pluripotency and differentiation by shp2 tyrosine phosphatase

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The molecular functions of Shp2 in the Ras/Mitogen-activated protein kinase (ERK1/2) pathway

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Neph1 cooperates with nephrin to transduce a signal that induces actin polymerization

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Design and implementation of bimolecular fluorescence complementation (BiFC) assays for the visualization of protein interactions in living cells

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Structure-based kinetic models of modular signaling protein function: focus on Shp2.

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SHP-2 activates signaling of the nuclear factor of activated T cells to promote skeletal muscle growth

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Discovery of a novel shp2 protein tyrosine phosphatase inhibitor

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30 September 2017

Intrinsic FAK activity and Y925 phosphorylation facilitate an angiogenic switch in tumors

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30 September 2017

Nephrin ectodomain engagement results in Src kinase activation, nephrin phosphorylation, Nck recruitment, and actin polymerization

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30 September 2017

Nck adaptor proteins link nephrin to the actin cytoskeleton of kidney podocytes

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30 September 2017

Multiple connections link FAK to cell motility and invasion

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30 September 2017

Inducible clustering of membrane-targeted SH3 domains of the adaptor protein Nck triggers localized actin polymerization

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30 September 2017

Clustering-induced tyrosine phosphorylation of nephrin by Src family kinases

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30 September 2017

The 'Shp'ing news: SH2 domain-containing tyrosine phosphatases in cell signaling

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30 September 2017

Fyn binds to and phosphorylates the kidney slit diaphragm component Nephrin

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Differential regulation of cell motility and invasion by FAK

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30 September 2017

Essential role of Gas6 for glomerular injury in nephrotoxic nephritis.

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The Nck family of adapter proteins: regulators of actin cytoskeleton

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30 September 2017

Site-specific incorporation of a phosphotyrosine mimetic reveals a role for tyrosine phosphorylation of SHP-2 in cell signaling

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30 September 2017

Regulation of mouse podocyte process dynamics by protein tyrosine phosphatases rapid communication

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Cre recombinase: the universal reagent for genome tailoring

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Lack of chemokine receptor CCR1 enhances Th1 responses and glomerular injury during nephrotoxic nephritis

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Shp-2 tyrosine phosphatase: signaling one cell or many

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Genetic evidence that Shp-2 tyrosine phosphatase is a signal enhancer of the epidermal growth factor receptor in mammals

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Regulation of early events in integrin signaling by protein tyrosine phosphatase SHP-2.

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Protein-tyrosine phosphatase Shp-2 regulates cell spreading, migration, and focal adhesion

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Abnormal mesoderm patterning in mouse embryos mutant for the SH2 tyrosine phosphatase Shp-2.

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Activation of the SH2-containing protein tyrosine phosphatase, SH-PTP2, by phosphotyrosine-containing peptides derived from insulin receptor substrate-1

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Phosphorylation of Nephrin Triggers Ca2+ Signaling by Recruitment and Activation of Phospholipase C-{gamma}1.

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Shp2 regulates SRC family kinase activity and Ras/Erk activation by controlling Csk recruitment

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Nephrin localizes to the slit pore of the glomerular epithelial cell

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Tyrosine kinase signalling pathways

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Potent stimulation of SH-PTP2 phosphatase activity by simultaneous occupancy of both SH2 domains

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12 December 2020

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10.1128/MCB.00956-15

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2 March 2020

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