Epithelial cell polarity: New perspectives

A. H. Le Gall, C. Yeaman, Anne Muesch, E. Rodriguez-Boulan

Research output: Contribution to journalArticle

41 Citations (Scopus)

Abstract

All epithelial cells possess two distinct plasma membrane domains. The apical and basolateral domains differ in protein and lipid composition, and this allows the cell to perform a variety of vectorial functions. Structures involved in generating and maintaining these distinct membrane domains include the tight junction, which serves to restrict lateral diffusion within the membrane, and the cortical cytoskeleton, which can selectively bind and retain transmembrane proteins at a particular surface. A major means to generating membrane asymmetry lies in the ability of the cell to sort apical and basolateral proteins and target them to appropriate destinations. This sorting occurs predominantly at two intracellular sites: the trans-Golgi network, and the basolateral endosome. Constitutive protein traffic in epithelial cells has recently been shown to be regulated via classical signal transduction pathways involving heterotrimeric G proteins and protein kinases. The diversion of apical and basolateral proteins into specific pathways can be mediated by signals contained within these proteins. Apical sorting information is thought to be localized in the luminal domain of transmembrane proteins, and in the case of proteins anchored to the membrane via a GPI anchor, apical sorting information is provided by the lipid moiety. In contrast, basolateral signals hove been identified in the cytoplasmic domain of transmembrane proteins. Shared similarities between basolateral signals and those required for endocytosis have suggested that these two sorting processes are mechanistically related.

Original languageEnglish (US)
Pages (from-to)272-284
Number of pages13
JournalSeminars in Nephrology
Volume15
Issue number4
StatePublished - 1995

Fingerprint

Cell Polarity
Epithelial Cells
Proteins
Membranes
trans-Golgi Network
Lipids
Heterotrimeric GTP-Binding Proteins
Tight Junctions
Endosomes
Endocytosis
Cytoskeleton
Protein Kinases
Signal Transduction
Cell Membrane

ASJC Scopus subject areas

  • Nephrology

Cite this

Le Gall, A. H., Yeaman, C., Muesch, A., & Rodriguez-Boulan, E. (1995). Epithelial cell polarity: New perspectives. Seminars in Nephrology, 15(4), 272-284.

Epithelial cell polarity : New perspectives. / Le Gall, A. H.; Yeaman, C.; Muesch, Anne; Rodriguez-Boulan, E.

In: Seminars in Nephrology, Vol. 15, No. 4, 1995, p. 272-284.

Research output: Contribution to journalArticle

Le Gall, AH, Yeaman, C, Muesch, A & Rodriguez-Boulan, E 1995, 'Epithelial cell polarity: New perspectives', Seminars in Nephrology, vol. 15, no. 4, pp. 272-284.
Le Gall AH, Yeaman C, Muesch A, Rodriguez-Boulan E. Epithelial cell polarity: New perspectives. Seminars in Nephrology. 1995;15(4):272-284.
Le Gall, A. H. ; Yeaman, C. ; Muesch, Anne ; Rodriguez-Boulan, E. / Epithelial cell polarity : New perspectives. In: Seminars in Nephrology. 1995 ; Vol. 15, No. 4. pp. 272-284.
@article{85e6b34a8dd74091b56fba53307045a5,
title = "Epithelial cell polarity: New perspectives",
abstract = "All epithelial cells possess two distinct plasma membrane domains. The apical and basolateral domains differ in protein and lipid composition, and this allows the cell to perform a variety of vectorial functions. Structures involved in generating and maintaining these distinct membrane domains include the tight junction, which serves to restrict lateral diffusion within the membrane, and the cortical cytoskeleton, which can selectively bind and retain transmembrane proteins at a particular surface. A major means to generating membrane asymmetry lies in the ability of the cell to sort apical and basolateral proteins and target them to appropriate destinations. This sorting occurs predominantly at two intracellular sites: the trans-Golgi network, and the basolateral endosome. Constitutive protein traffic in epithelial cells has recently been shown to be regulated via classical signal transduction pathways involving heterotrimeric G proteins and protein kinases. The diversion of apical and basolateral proteins into specific pathways can be mediated by signals contained within these proteins. Apical sorting information is thought to be localized in the luminal domain of transmembrane proteins, and in the case of proteins anchored to the membrane via a GPI anchor, apical sorting information is provided by the lipid moiety. In contrast, basolateral signals hove been identified in the cytoplasmic domain of transmembrane proteins. Shared similarities between basolateral signals and those required for endocytosis have suggested that these two sorting processes are mechanistically related.",
author = "{Le Gall}, {A. H.} and C. Yeaman and Anne Muesch and E. Rodriguez-Boulan",
year = "1995",
language = "English (US)",
volume = "15",
pages = "272--284",
journal = "Seminars in Nephrology",
issn = "0270-9295",
publisher = "W.B. Saunders Ltd",
number = "4",

}

TY - JOUR

T1 - Epithelial cell polarity

T2 - New perspectives

AU - Le Gall, A. H.

AU - Yeaman, C.

AU - Muesch, Anne

AU - Rodriguez-Boulan, E.

PY - 1995

Y1 - 1995

N2 - All epithelial cells possess two distinct plasma membrane domains. The apical and basolateral domains differ in protein and lipid composition, and this allows the cell to perform a variety of vectorial functions. Structures involved in generating and maintaining these distinct membrane domains include the tight junction, which serves to restrict lateral diffusion within the membrane, and the cortical cytoskeleton, which can selectively bind and retain transmembrane proteins at a particular surface. A major means to generating membrane asymmetry lies in the ability of the cell to sort apical and basolateral proteins and target them to appropriate destinations. This sorting occurs predominantly at two intracellular sites: the trans-Golgi network, and the basolateral endosome. Constitutive protein traffic in epithelial cells has recently been shown to be regulated via classical signal transduction pathways involving heterotrimeric G proteins and protein kinases. The diversion of apical and basolateral proteins into specific pathways can be mediated by signals contained within these proteins. Apical sorting information is thought to be localized in the luminal domain of transmembrane proteins, and in the case of proteins anchored to the membrane via a GPI anchor, apical sorting information is provided by the lipid moiety. In contrast, basolateral signals hove been identified in the cytoplasmic domain of transmembrane proteins. Shared similarities between basolateral signals and those required for endocytosis have suggested that these two sorting processes are mechanistically related.

AB - All epithelial cells possess two distinct plasma membrane domains. The apical and basolateral domains differ in protein and lipid composition, and this allows the cell to perform a variety of vectorial functions. Structures involved in generating and maintaining these distinct membrane domains include the tight junction, which serves to restrict lateral diffusion within the membrane, and the cortical cytoskeleton, which can selectively bind and retain transmembrane proteins at a particular surface. A major means to generating membrane asymmetry lies in the ability of the cell to sort apical and basolateral proteins and target them to appropriate destinations. This sorting occurs predominantly at two intracellular sites: the trans-Golgi network, and the basolateral endosome. Constitutive protein traffic in epithelial cells has recently been shown to be regulated via classical signal transduction pathways involving heterotrimeric G proteins and protein kinases. The diversion of apical and basolateral proteins into specific pathways can be mediated by signals contained within these proteins. Apical sorting information is thought to be localized in the luminal domain of transmembrane proteins, and in the case of proteins anchored to the membrane via a GPI anchor, apical sorting information is provided by the lipid moiety. In contrast, basolateral signals hove been identified in the cytoplasmic domain of transmembrane proteins. Shared similarities between basolateral signals and those required for endocytosis have suggested that these two sorting processes are mechanistically related.

UR - http://www.scopus.com/inward/record.url?scp=0029020552&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0029020552&partnerID=8YFLogxK

M3 - Article

C2 - 7569407

AN - SCOPUS:0029020552

VL - 15

SP - 272

EP - 284

JO - Seminars in Nephrology

JF - Seminars in Nephrology

SN - 0270-9295

IS - 4

ER -