Guilt by association: what p120-catenin has to hide

Publikation: Bidrag til tidsskrift › Kommentar/debat › Forskning › fagfællebedømt

Standard

Guilt by association : what p120-catenin has to hide. / Perez-Moreno, Mirna; Fuchs, Elaine.

I: Journal of Cell Biology, Bind 199, Nr. 2, 2012, s. 211-214.

Publikation: Bidrag til tidsskrift › Kommentar/debat › Forskning › fagfællebedømt

Harvard

Perez-Moreno, M & Fuchs, E 2012, 'Guilt by association: what p120-catenin has to hide', Journal of Cell Biology, bind 199, nr. 2, s. 211-214. https://doi.org/10.1083/jcb.201209014

APA

Perez-Moreno, M., & Fuchs, E. (2012). Guilt by association: what p120-catenin has to hide. Journal of Cell Biology, 199(2), 211-214. https://doi.org/10.1083/jcb.201209014

Vancouver

Perez-Moreno M, Fuchs E. Guilt by association: what p120-catenin has to hide. Journal of Cell Biology. 2012;199(2):211-214. https://doi.org/10.1083/jcb.201209014

Author

Perez-Moreno, Mirna ; Fuchs, Elaine. / Guilt by association : what p120-catenin has to hide. I: Journal of Cell Biology. 2012 ; Bind 199, Nr. 2. s. 211-214.

Bibtex

@article{dc3e18c0db5e464abc3acb536a723a30,
title = "Guilt by association: what p120-catenin has to hide",
abstract = "Members of the p120-catenin family associate with cadherins and regulate their stability at the plasma membrane. How p120-catenin limits cadherin endocytosis has long remained a mystery. In this issue, Nanes et al. (2012. J. Cell Biol. doi:10.1083/jcb.201205029) identify a conserved acidic motif within cadherins that acts as a physical platform for p120-catenin binding. However, in the absence of p120-catenin, the motif acts as an endocytic signal. These results provide new insight into p120-catenin's role as guardian of intercellular junction dynamics.",
keywords = "Adherens Junctions, Animals, Antigens, CD, Cadherins, Catenins, Endocytosis, Humans, Comment, Journal Article, Research Support, N.I.H., Extramural, Research Support, Non-U.S. Gov't",
author = "Mirna Perez-Moreno and Elaine Fuchs",
year = "2012",
doi = "10.1083/jcb.201209014",
language = "English",
volume = "199",
pages = "211--214",
journal = "Journal of Cell Biology",
issn = "0021-9525",
publisher = "Rockefeller University Press",
number = "2",

}

RIS

TY - JOUR

T1 - Guilt by association

T2 - what p120-catenin has to hide

AU - Perez-Moreno, Mirna

AU - Fuchs, Elaine

PY - 2012

Y1 - 2012

N2 - Members of the p120-catenin family associate with cadherins and regulate their stability at the plasma membrane. How p120-catenin limits cadherin endocytosis has long remained a mystery. In this issue, Nanes et al. (2012. J. Cell Biol. doi:10.1083/jcb.201205029) identify a conserved acidic motif within cadherins that acts as a physical platform for p120-catenin binding. However, in the absence of p120-catenin, the motif acts as an endocytic signal. These results provide new insight into p120-catenin's role as guardian of intercellular junction dynamics.

AB - Members of the p120-catenin family associate with cadherins and regulate their stability at the plasma membrane. How p120-catenin limits cadherin endocytosis has long remained a mystery. In this issue, Nanes et al. (2012. J. Cell Biol. doi:10.1083/jcb.201205029) identify a conserved acidic motif within cadherins that acts as a physical platform for p120-catenin binding. However, in the absence of p120-catenin, the motif acts as an endocytic signal. These results provide new insight into p120-catenin's role as guardian of intercellular junction dynamics.

KW - Adherens Junctions

KW - Animals

KW - Antigens, CD

KW - Cadherins

KW - Catenins

KW - Endocytosis

KW - Humans

KW - Comment

KW - Journal Article

KW - Research Support, N.I.H., Extramural

KW - Research Support, Non-U.S. Gov't

U2 - 10.1083/jcb.201209014

DO - 10.1083/jcb.201209014

M3 - Comment/debate

C2 - 23071151

VL - 199

SP - 211

EP - 214

JO - Journal of Cell Biology

JF - Journal of Cell Biology

SN - 0021-9525

IS - 2

ER -

ID: 188368581