Nephrin binds to the COOH terminus of a large-conductance Ca2+-activated K+ channel isoform and regulates its expression on the cell surface (Q36807046)

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scientific article published on 14 May 2008

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English	Nephrin binds to the COOH terminus of a large-conductance Ca2+-activated K+ channel isoform and regulates its expression on the cell surface	scientific article published on 14 May 2008

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scholarly article

1 reference

Europe PubMed Central

PMC publication ID

16 August 2017

Nephrin binds to the COOH terminus of a large-conductance Ca2+-activated K+ channel isoform and regulates its expression on the cell surface (English)

1 reference

Europe PubMed Central

PMC publication ID

16 August 2017

author name string

Eun Young Kim

1

1 reference

Europe PubMed Central

PMC publication ID

16 August 2017

Kyoung-Jae Choi

2

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Europe PubMed Central

PMC publication ID

16 August 2017

Stuart E Dryer

3

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Europe PubMed Central

PMC publication ID

16 August 2017

language of work or name

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publication date

14 May 2008

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Europe PubMed Central

PMC publication ID

16 August 2017

American Journal of Physiology - Renal Physiology

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Europe PubMed Central

PMC publication ID

16 August 2017

295

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Europe PubMed Central

PMC publication ID

16 August 2017

1

1 reference

Europe PubMed Central

PMC publication ID

16 August 2017

F235-46

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Europe PubMed Central

PMC publication ID

16 August 2017

describes a project that uses

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Europe PubMed Central

11 June 2022

https://www.ebi.ac.uk/europepmc/webservices/rest/PMC2494500/fullTextXML

based on heuristic

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A novel actin-binding domain on Slo1 calcium-activated potassium channels is necessary for their expression in the plasma membrane

1 reference

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

1 reference

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1 reference

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1 reference

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Interactions with filamin A stimulate surface expression of large-conductance Ca2+-activated K+ channels in the absence of direct actin binding

1 reference

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Beta1-subunits increase surface expression of a large-conductance Ca2+-activated K+ channel isoform

1 reference

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Differential trafficking of carboxyl isoforms of Ca2+-gated (Slo1) potassium channels

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1 reference

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

1 reference

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1 reference

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pH sensing in the two-pore domain K+ channel, TASK2.

1 reference

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1 reference

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Human podocytes possess a stretch-sensitive, Ca2+-activated K+ channel: potential implications for the control of glomerular filtration

1 reference

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Nephrin forms a complex with adherens junction proteins and CASK in podocytes and in Madin-Darby canine kidney cells expressing nephrin

1 reference

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Deletion of the Ca2+-activated potassium (BK) alpha-subunit but not the BKbeta1-subunit leads to progressive hearing loss

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1 reference

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Nephrin and CD2AP associate with phosphoinositide 3-OH kinase and stimulate AKT-dependent signaling

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Cell biology of the glomerular podocyte

1 reference

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The cytoplasmic tail of large conductance, voltage- and Ca2+-activated K+ (MaxiK) channel is necessary for its cell surface expression

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Podocin, a raft-associated component of the glomerular slit diaphragm, interacts with CD2AP and nephrin

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CD2AP localizes to the slit diaphragm and binds to nephrin via a novel C-terminal domain

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Interaction with podocin facilitates nephrin signaling

1 reference

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1 reference

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1 reference

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1 reference

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Nephrin Is Critical for the Action of Insulin on Human Glomerular Podocytes

1 reference

https://pubmed.ncbi.nlm.nih.gov/18480178

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1152/AJPRENAL.00140.2008

1 reference

Europe PubMed Central

PMC publication ID

16 August 2017

PMC publication ID

1 reference

Europe PubMed Central

PMC publication ID

16 August 2017

PubMed publication ID

1 reference

Europe PubMed Central

PMC publication ID

16 August 2017

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