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Reviews of Physiology, Biochemistry and Pharmacology pp 47–99Cite as

Molecular mechanisms of membrane polarity in renal epithelial cells

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Part of the book series: Reviews of Physiology, Biochemistry and Pharmacology ((REVIEWS,volume 153))

Abstract

Exciting discoveries in the last decade have cast light onto the fundamental mechanisms that underlie polarized trafficking in epithelial cells. It is now clear that epithelial cell membrane asymmetry is achieved by a combination of intracellular sorting operations, vectorial delivery mechanisms and plasmalemma-specific fusion and retention processes. Several well-defined signals that specify polarized segregation, sorting, or retention processes have, now, been described in a number of proteins. The intracellular machineries that decode and act on these signals are beginning to be described. In addition, the nature of the molecules that associate with intracellular trafficking vesicles to coordinate polarized delivery, tethering, docking, and fusion are also becoming understood. Combined with direct visualization of polarized sorting processes with new technologies in live-cell fluorescent microscopy, new and surprising insights into these once-elusive trafficking processes are emerging. Here we provide a review of these recent advances within an historically relevant context.

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Abbreviations

AEE:

Apical Early Endosomes

AP:

Adaptins or clathrin-adaptor complexes

ARF:

ADP-ribosylation factor, Ras-like small G-proteins involved in vesicular trafficking

BFA:

Brefeldin A, a fungal metabolite that inhibits ARF-dependent attachment of coat proteins

BEE:

Basolateral Early Endosomes

CASK:

Calcium/calmodulin-dependent protein kinase, MAGUK protein, also known as Lin-2

CRE:

Common Recycling Endosome

DRM:

Detergent Resistant Membrane, a biochemical hallmark of a raft

ECM:

Extracellular Matrix

EEA1:

Early Endosome Antigen 1, a Rab effector and a marker for the early endosome

FYVE:

Zinc-binding domain named after the proteins that it is found in; targets proteins to membrane lipids via interaction with phosphatidylinositol-3-phosphate, “PI3P finger protein”

GFP:

Green Fluorescent Protein

GPI:

Glycosyl Phosphatidyl Inositol

HA:

Influenza Hemagglutinin, a prototypical apical marker protein

MDCK:

Madin Darby Kidney Cells, a polarized epithelial cell line

Munc18—1:

Mammalian UNC18, C. ELEGANS, syntaxin-binding protein 1

LDLR:

Low-Density Lipoprotein Receptor, a prototypical basolateral marker

LLC-PK1:

A pig kidney polarized epithelial cell model

L27:

A protein—protein interaction domain first identified in Lin-2 and Lin-7

Lin:

Genes that were first identified in genetic screens for abnormal cell lineage in C. Elegans

MAGUK:

Membrane Associated Guanlyate Kinases, a family of PDZ proteins

MT:

Microtubule

NSF:

N-ethyl maleimide-sensitive factor, a component of the fusion machinery

pIgR:

Polymeric Immunoglobin Receptor For IgA, a prototypical protein for basolateral to apical transcytosis

Par:

Partitioning Defective Proteins

PDZ:

A protein—protein interaction domain found in scaffolding proteins

PGTI:

Post-Golgi transport intermediates

Rab:

A family of RAS-related small GTP-binding proteins that play important roles in the regulation of exocytotic and endocytotic pathway

Ral:

A family of RAS-related small GTP-binding proteins that have been implicated in vesicle trafficking, cell morphology, and signalling

TfR:

Transferrin receptor, a prototypical marker for basolateral membrane and CRE recycling

SAC:

Subapical Compartment, also known as ARE

Sec 6/8:

Components of the exocyst, but the term is often used to refer to the entire mammalian exocyst complex

SNAP:

Soluble NSF Attachment Factor, component of fusion machinery

SNARE:

Soluble N-Ethyl Maleimide-Sensitive Attachment Factor Receptors, components of fusion machinery

t-SNARE:

SNARES on target membrane

v-SNARE:

SNARES on vesicle membrane, also known as VAMP/synaptobrevin

TGN:

Trans-Golgi Network

VAMP:

Vesicle Associated Membrane Protein, also known as v-SNARE

VSV G:

Vesicular Stomatitis Virus coat protein, used as a prototypical basolateral marker

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Authors and Affiliations

  1. Department of Physiology, University of Maryland School of Medicine, Baltimore, MD, 21201, USA

    C. Campo, A. Mason, D. Maouyo, O. Olsen, D. Yoo & P. A. Welling

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  1. C. Campo
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  2. A. Mason
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  3. D. Maouyo
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  4. O. Olsen
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  5. D. Yoo
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  6. P. A. Welling
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Campo, C., Mason, A., Maouyo, D., Olsen, O., Yoo, D., Welling, P.A. (2005). Molecular mechanisms of membrane polarity in renal epithelial cells. In: Reviews of Physiology, Biochemistry and Pharmacology. Reviews of Physiology, Biochemistry and Pharmacology, vol 153. Springer, Berlin, Heidelberg. https://doi.org/10.1007/s10254-004-0037-1

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