Stabilization of cell polarity by the C. elegans RING protein PAR-2

Yingsong Hao, Lynn Boyd, Geraldine Seydoux

Research output: Contribution to journalArticle

Abstract

Asymmetric localization of PAR proteins is a hallmark of polarized cells, but the mechanisms that create PAR asymmetry are not well understood. In the C. elegans zygote, PAR asymmetry is initiated by a transient actomyosin contraction, which sweeps the PAR-3/PAR-6/PKC-3 complex toward the anterior pole of the egg. The RING finger protein PAR-2 accumulates in a complementary pattern in the posterior cortex. Here we present evidence that PAR-2 participates in a feedback loop to stabilize polarity. PAR-2 is a target of the PKC-3 kinase and is excluded from the anterior cortex by PKC-3-dependent phosphorylation. The RING domain of PAR-2 is required to overcome inhibition by PKC-3 and stabilize PAR-2 on the posterior cortex. Cortical PAR-2 in turn prevents PAR-3/PAR-6/PKC-3 from returning to the posterior, in a PAR-1- and PAR-5-dependent manner. Our findings suggest that reciprocal inhibitory interactions among PAR proteins stabilize polarity by reinforcing an initial asymmetry in PKC-3.

Original languageEnglish (US)
Pages (from-to)199-208
Number of pages10
JournalDevelopmental Cell
Volume10
Issue number2
DOIs
StatePublished - Feb 2006

Fingerprint

Caenorhabditis elegans Proteins
Cell Polarity
Stabilization
Actomyosin
Phosphorylation
Proteins
Zygote
Ovum
Poles
Phosphotransferases
Feedback

Keywords

  • Cellbio
  • Devbio
  • Proteins

ASJC Scopus subject areas

  • Developmental Biology

Cite this

Stabilization of cell polarity by the C. elegans RING protein PAR-2. / Hao, Yingsong; Boyd, Lynn; Seydoux, Geraldine.

In: Developmental Cell, Vol. 10, No. 2, 02.2006, p. 199-208.

Research output: Contribution to journalArticle

Hao, Yingsong ; Boyd, Lynn ; Seydoux, Geraldine. / Stabilization of cell polarity by the C. elegans RING protein PAR-2. In: Developmental Cell. 2006 ; Vol. 10, No. 2. pp. 199-208.
@article{8bf0b01e44944d4ebc7434b196c44793,
title = "Stabilization of cell polarity by the C. elegans RING protein PAR-2",
abstract = "Asymmetric localization of PAR proteins is a hallmark of polarized cells, but the mechanisms that create PAR asymmetry are not well understood. In the C. elegans zygote, PAR asymmetry is initiated by a transient actomyosin contraction, which sweeps the PAR-3/PAR-6/PKC-3 complex toward the anterior pole of the egg. The RING finger protein PAR-2 accumulates in a complementary pattern in the posterior cortex. Here we present evidence that PAR-2 participates in a feedback loop to stabilize polarity. PAR-2 is a target of the PKC-3 kinase and is excluded from the anterior cortex by PKC-3-dependent phosphorylation. The RING domain of PAR-2 is required to overcome inhibition by PKC-3 and stabilize PAR-2 on the posterior cortex. Cortical PAR-2 in turn prevents PAR-3/PAR-6/PKC-3 from returning to the posterior, in a PAR-1- and PAR-5-dependent manner. Our findings suggest that reciprocal inhibitory interactions among PAR proteins stabilize polarity by reinforcing an initial asymmetry in PKC-3.",
keywords = "Cellbio, Devbio, Proteins",
author = "Yingsong Hao and Lynn Boyd and Geraldine Seydoux",
year = "2006",
month = "2",
doi = "10.1016/j.devcel.2005.12.015",
language = "English (US)",
volume = "10",
pages = "199--208",
journal = "Developmental Cell",
issn = "1534-5807",
publisher = "Cell Press",
number = "2",

}

TY - JOUR

T1 - Stabilization of cell polarity by the C. elegans RING protein PAR-2

AU - Hao, Yingsong

AU - Boyd, Lynn

AU - Seydoux, Geraldine

PY - 2006/2

Y1 - 2006/2

N2 - Asymmetric localization of PAR proteins is a hallmark of polarized cells, but the mechanisms that create PAR asymmetry are not well understood. In the C. elegans zygote, PAR asymmetry is initiated by a transient actomyosin contraction, which sweeps the PAR-3/PAR-6/PKC-3 complex toward the anterior pole of the egg. The RING finger protein PAR-2 accumulates in a complementary pattern in the posterior cortex. Here we present evidence that PAR-2 participates in a feedback loop to stabilize polarity. PAR-2 is a target of the PKC-3 kinase and is excluded from the anterior cortex by PKC-3-dependent phosphorylation. The RING domain of PAR-2 is required to overcome inhibition by PKC-3 and stabilize PAR-2 on the posterior cortex. Cortical PAR-2 in turn prevents PAR-3/PAR-6/PKC-3 from returning to the posterior, in a PAR-1- and PAR-5-dependent manner. Our findings suggest that reciprocal inhibitory interactions among PAR proteins stabilize polarity by reinforcing an initial asymmetry in PKC-3.

AB - Asymmetric localization of PAR proteins is a hallmark of polarized cells, but the mechanisms that create PAR asymmetry are not well understood. In the C. elegans zygote, PAR asymmetry is initiated by a transient actomyosin contraction, which sweeps the PAR-3/PAR-6/PKC-3 complex toward the anterior pole of the egg. The RING finger protein PAR-2 accumulates in a complementary pattern in the posterior cortex. Here we present evidence that PAR-2 participates in a feedback loop to stabilize polarity. PAR-2 is a target of the PKC-3 kinase and is excluded from the anterior cortex by PKC-3-dependent phosphorylation. The RING domain of PAR-2 is required to overcome inhibition by PKC-3 and stabilize PAR-2 on the posterior cortex. Cortical PAR-2 in turn prevents PAR-3/PAR-6/PKC-3 from returning to the posterior, in a PAR-1- and PAR-5-dependent manner. Our findings suggest that reciprocal inhibitory interactions among PAR proteins stabilize polarity by reinforcing an initial asymmetry in PKC-3.

KW - Cellbio

KW - Devbio

KW - Proteins

UR - http://www.scopus.com/inward/record.url?scp=31744439314&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=31744439314&partnerID=8YFLogxK

U2 - 10.1016/j.devcel.2005.12.015

DO - 10.1016/j.devcel.2005.12.015

M3 - Article

C2 - 16459299

AN - SCOPUS:31744439314

VL - 10

SP - 199

EP - 208

JO - Developmental Cell

JF - Developmental Cell

SN - 1534-5807

IS - 2

ER -