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Trans-interaction of nephrin and Neph1/Neph3 induces cell adhesion that associates with decreased tyrosine phosphorylation of nephrin

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Trans-interaction of nephrin and Neph1/Neph3 induces cell adhesion that associates with decreased tyrosine phosphorylation of nephrin. / Heikkilä, Eija; Ristola, Mervi; Havana, Marika; Jones, Nina; Holthöfer, Harry; Lehtonen, Sanna.

In: BIOCHEMICAL JOURNAL, Vol. 435, No. 3, 01.05.2011, p. 619-628.

Research output: Contribution to journalArticleScientificpeer-review

Harvard

Heikkilä, E, Ristola, M, Havana, M, Jones, N, Holthöfer, H & Lehtonen, S 2011, 'Trans-interaction of nephrin and Neph1/Neph3 induces cell adhesion that associates with decreased tyrosine phosphorylation of nephrin', BIOCHEMICAL JOURNAL, vol. 435, no. 3, pp. 619-628. https://doi.org/10.1042/BJ20101599

APA

Heikkilä, E., Ristola, M., Havana, M., Jones, N., Holthöfer, H., & Lehtonen, S. (2011). Trans-interaction of nephrin and Neph1/Neph3 induces cell adhesion that associates with decreased tyrosine phosphorylation of nephrin. BIOCHEMICAL JOURNAL, 435(3), 619-628. https://doi.org/10.1042/BJ20101599

Vancouver

Heikkilä E, Ristola M, Havana M, Jones N, Holthöfer H, Lehtonen S. Trans-interaction of nephrin and Neph1/Neph3 induces cell adhesion that associates with decreased tyrosine phosphorylation of nephrin. BIOCHEMICAL JOURNAL. 2011 May 1;435(3):619-628. https://doi.org/10.1042/BJ20101599

Author

Heikkilä, Eija ; Ristola, Mervi ; Havana, Marika ; Jones, Nina ; Holthöfer, Harry ; Lehtonen, Sanna. / Trans-interaction of nephrin and Neph1/Neph3 induces cell adhesion that associates with decreased tyrosine phosphorylation of nephrin. In: BIOCHEMICAL JOURNAL. 2011 ; Vol. 435, No. 3. pp. 619-628.

Bibtex - Download

@article{b79cd5845690410da34cad886bc8c027,
title = "Trans-interaction of nephrin and Neph1/Neph3 induces cell adhesion that associates with decreased tyrosine phosphorylation of nephrin",
abstract = "Slit diaphragms are specialized junctions between glomerular epithelial cells (podocytes) that are crucial for glomerular ultrafiltration. The Ig superfamily members nephrin and Neph1 are essential components of the slit diaphragm, whereas the role of Neph1 homologue Neph3 in the slit diaphragm is unknown. In the present paper we show that Neph3 homodimerizes and heterodimerizes with nephrin and Neph1.We further investigated whether these interactions play a role in cell adhesion by using mouse L fibroblasts that lack endogenous cell-adhesion activity and found that Neph1 and Neph3 are able to induce cell adhesion alone, whereas nephrin needs to trans-interact with Neph1 or Neph3 in order to promote formation of cell - cell contacts. Tyrosine phosphorylation of nephrin was down-regulated after nephrin trans-interacted with either Neph1 or Neph3 leading to formation of cell - cell contacts. We further found that the expression of Neph3 was increased in nephrin-deficient mouse podocytes. The findings of the present paper show that nephrin and Neph1 or Neph3 trans-interactions promote cell-contact formation, suggesting that they may also function together in slit diaphragm assembly.",
keywords = "Cell - cell contact, Neph family, Nephrin, Podocyte, Slit diaphragm",
author = "Eija Heikkil{\"a} and Mervi Ristola and Marika Havana and Nina Jones and Harry Holth{\"o}fer and Sanna Lehtonen",
year = "2011",
month = "5",
day = "1",
doi = "10.1042/BJ20101599",
language = "English",
volume = "435",
pages = "619--628",
journal = "BIOCHEMICAL JOURNAL",
issn = "0264-6021",
publisher = "Portland Press",
number = "3",

}

RIS (suitable for import to EndNote) - Download

TY - JOUR

T1 - Trans-interaction of nephrin and Neph1/Neph3 induces cell adhesion that associates with decreased tyrosine phosphorylation of nephrin

AU - Heikkilä, Eija

AU - Ristola, Mervi

AU - Havana, Marika

AU - Jones, Nina

AU - Holthöfer, Harry

AU - Lehtonen, Sanna

PY - 2011/5/1

Y1 - 2011/5/1

N2 - Slit diaphragms are specialized junctions between glomerular epithelial cells (podocytes) that are crucial for glomerular ultrafiltration. The Ig superfamily members nephrin and Neph1 are essential components of the slit diaphragm, whereas the role of Neph1 homologue Neph3 in the slit diaphragm is unknown. In the present paper we show that Neph3 homodimerizes and heterodimerizes with nephrin and Neph1.We further investigated whether these interactions play a role in cell adhesion by using mouse L fibroblasts that lack endogenous cell-adhesion activity and found that Neph1 and Neph3 are able to induce cell adhesion alone, whereas nephrin needs to trans-interact with Neph1 or Neph3 in order to promote formation of cell - cell contacts. Tyrosine phosphorylation of nephrin was down-regulated after nephrin trans-interacted with either Neph1 or Neph3 leading to formation of cell - cell contacts. We further found that the expression of Neph3 was increased in nephrin-deficient mouse podocytes. The findings of the present paper show that nephrin and Neph1 or Neph3 trans-interactions promote cell-contact formation, suggesting that they may also function together in slit diaphragm assembly.

AB - Slit diaphragms are specialized junctions between glomerular epithelial cells (podocytes) that are crucial for glomerular ultrafiltration. The Ig superfamily members nephrin and Neph1 are essential components of the slit diaphragm, whereas the role of Neph1 homologue Neph3 in the slit diaphragm is unknown. In the present paper we show that Neph3 homodimerizes and heterodimerizes with nephrin and Neph1.We further investigated whether these interactions play a role in cell adhesion by using mouse L fibroblasts that lack endogenous cell-adhesion activity and found that Neph1 and Neph3 are able to induce cell adhesion alone, whereas nephrin needs to trans-interact with Neph1 or Neph3 in order to promote formation of cell - cell contacts. Tyrosine phosphorylation of nephrin was down-regulated after nephrin trans-interacted with either Neph1 or Neph3 leading to formation of cell - cell contacts. We further found that the expression of Neph3 was increased in nephrin-deficient mouse podocytes. The findings of the present paper show that nephrin and Neph1 or Neph3 trans-interactions promote cell-contact formation, suggesting that they may also function together in slit diaphragm assembly.

KW - Cell - cell contact

KW - Neph family

KW - Nephrin

KW - Podocyte

KW - Slit diaphragm

UR - http://www.scopus.com/inward/record.url?scp=79954471298&partnerID=8YFLogxK

U2 - 10.1042/BJ20101599

DO - 10.1042/BJ20101599

M3 - Article

VL - 435

SP - 619

EP - 628

JO - BIOCHEMICAL JOURNAL

JF - BIOCHEMICAL JOURNAL

SN - 0264-6021

IS - 3

ER -