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 V O LU M E T WO S I X T Y F I V E

INTERNATIONAL REVIEW OF
CYTOLOGY
A Survey of Cell Biology
INTERNATIONAL REVIEW
OF CYTOLOGY
Series Editors

GEOFFREY H. BOURNE 1949–1988

JAMES F. DANIELLI 1949–1984
KWANG W. JEON 1967–
MARTIN FRIEDLANDER 1984–1992
JONATHAN JARVIK 1993–1995

Editorial Advisory Board

ISAIAH ARKIN WALLACE F. MARSHALL

EVE IDA BARAK BRUCE D. MCKEE
PETER L. BEECH MICHAEL MELKONIAN
HOWARD A. BERN KEITH E. MOSTOV
ROBERT A. BLOODGOOD ANDREAS OKSCHE
DEAN BOK THORU PEDERSON
HIROO FUKUDA MANFRED SCHLIWA
RAY H. GAVIN TERUO SHIMMEN
MAY GRIFFITH ROBERT A. SMITH
WILLIAM R. JEFFERY NIKOLAI TOMILIN
KEITH LATHAM
 V O LU M E T WO S I X T Y F I V E

INTERNATIONAL REVIEW OF
CYTOLOGY
A Survey of Cell Biology

EDITED BY

KWANG W. JEON
Department of Biochemistry
University of Tennessee
Knoxville, Tennessee

AMSTERDAM • BOSTON • HEIDELBERG • LONDON

NEW YORK • OXFORD • PARIS • SAN DIEGO
SAN FRANCISCO • SINGAPORE • SYDNEY • TOKYO
Academic Press is an imprint of Elsevier
Front Cover Photograph: Courtesy of Victor Shahin: Institute of Physiology II,
University of Muenster, Germany.

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PRINTED IN THE UNITED STATES OF AMERICA

08 09 10 11 12 8 7 6 5 4 3 2 1
CONTENTS

Contributors vii

1. Cross-Talk Among Integrin, Cadherin, and Growth Factor Receptor:

Roles of Nectin and Nectin-Like Molecule 1
Hisakazu Ogita and Yoshimi Takai
1. Introduction 2
2. Molecular and Structural Features of Nectin and Nectin-Like Molecule 4
3. Formation of Adherens Junctions Induced by the Nectin–Afadin System 9
4. Formation of Tight Junctions Regulated by the Nectin–Afadin System 22
5. Roles of Nectin and Necl-5 27
6. Common Utilization of Signaling Molecules in Forming Leading Edges
and Cell–Cell Adhesion 39
7. Concluding Remarks 40
References 41

2. Neural Stem Cells in the Mammalian Brain 55

A. V. Revishchin, L. I. Korochkin, V. E. Okhotin, and G. V. Pavlova
1. Introduction 56
2. Neural Stem Cells and Their Niches in the Adult Mammalian Brain 57
3. Transcriptional Regulation of NSC Self-Renewal and Differentiation 68
4. Neural Stem and Progenitor Cell-Based Therapy 82
5. Conclusions 90
Acknowledgments 91
References 91

3. Mechanisms of Mitotic Spindle Assembly and Function 111

Claire E. Walczak and Rebecca Heald

1. Introduction 112
2. Molecular Components of the Mitotic Spindle 113
3. Major Pathways of Spindle Assembly 119
4. Mechanisms of Chromosome Congression and Attachment 129
5. Mechanisms of Chromosome Segregation 138
6. Conclusions and Future Directions 143
Acknowledgments 144
References 144

v
vi Contents

4. Multiple Actions of Secretin in the Human Body 159

Ian P. Y. Lam, Francis K. Y. Siu, Jessica Y. S. Chu, and Billy K. C. Chow
1. Introduction 160
2. Structure and Regulation of Secretin and the Gene 163
3. Secretin’s Actions in the Gastrointestinal Tract 164
4. Secretin’s Actions in Other Tissues 172
5. Summary and Future Prospects 178
References 179

5. Biology of the Striated Muscle Dystrophin–Glycoprotein Complex 191

James M. Ervasti and Kevin J. Sonnemann
1. Introduction 192
2. Composition of the Core Dystrophin–Glycoprotein Complex 192
3. Function in Mammals 195
4. Function in Model Organisms 205
5. Concluding Remarks 207
Acknowledgments 208
References 208

6. Providing Unique Insight into Cell Biology via Atomic

Force Microscopy 227
Victor Shahin and Nelson P. Barrera
1. Introduction 228
2. AFM: Principle of Operation and Operation Modes 229
3. AFM Can Measure Forces and Elasticity 232
4. Advantages of AFM 234
5. Application of AFM to Biology 235
6. Conclusions 246
Acknowledgments 247
References 247

7. Characteristics of Oxysterol Binding Proteins 253

Daoguang Yan and Vesa M. Olkkonen

1. Introduction 254
2. Subcellular Distribution of the ORPs 258
3. Role of the Mammalian ORPs in Lipid Metabolism 262
4. The Yeast S. cerevisiae ORPs 269
5. Role of ORPs in Cell Signaling 272
6. Future Perspectives 274
Acknowledgments 276
References 277

Index 287
CONTRIBUTORS

Nelson P. Barrera
Department of Chemistry, University of Cambridge, Cambridge CB2 1EW,
United Kingdom
Billy K. C. Chow
Department of Zoology, University of Hong Kong, Hong Kong, China
Jessica Y. S. Chu
Department of Zoology, University of Hong Kong, Hong Kong, China
James M. Ervasti
Department of Biochemistry, Molecular Biology and Biophysics, University of
Minnesota, Minneapolis, Minnesota 55455
Rebecca Heald
Molecular and Cell Biology Department, University of California, Berkeley,
California 94720
L. I. Korochkin
Institute of Gene Biology, Russian Academy of Sciences, Moscow, 119334 Russia
Ian P. Y. Lam
Department of Zoology, University of Hong Kong, Hong Kong, China
Hisakazu Ogita
Department of Molecular Biology and Biochemistry, Osaka University Graduate
School of Medicine/Faculty of Medicine, Suita, Osaka 565-0871, Japan
V. E. Okhotin
Institute of Gene Biology, Russian Academy of Sciences, Moscow, 119334 Russia
Vesa M. Olkkonen
Department of Molecular Medicine, National Public Health Institute, Biomedicum,
FI-00290 Helsinki, Finland
G. V. Pavlova
Institute of Gene Biology, Russian Academy of Sciences, Moscow, 119334 Russia
A. V. Revishchin
Institute of Gene Biology, Russian Academy of Sciences, Moscow, 119334 Russia
and Severtsov Institute of Ecology and Evolution, Russian Academy of Sciences,
Moscow, 119071 Russia

vii
viii Contributors

Victor Shahin
Institute of Physiology II, University of Muenster, D-48149 Muenster, Germany
Francis K. Y. Siu
Department of Zoology, University of Hong Kong, Hong Kong, China
Kevin J. Sonnemann
Department of Biochemistry, Molecular Biology and Biophysics, University of
Minnesota, Minneapolis, Minnesota 55455
Yoshimi Takai
Department of Molecular Biology and Biochemistry, Osaka University Graduate
School of Medicine/Faculty of Medicine, Suita, Osaka 565-0871, Japan
Claire E. Walczak
Medical Sciences Program, Indiana University, Bloomington, Indiana 47405
Daoguang Yan
Department of Molecular Medicine, National Public Health Institute, Biomedicum,
FI-00290 Helsinki, Finland
 C H A P T E R O N E

Cross-Talk Among Integrin,

Cadherin, and Growth Factor
Receptor: Roles of Nectin and
Nectin-Like Molecule
Hisakazu Ogita and Yoshimi Takai

Contents
1. Introduction 2
2. Molecular and Structural Features of Nectin and
Nectin-Like Molecule 4
3. Formation of Adherens Junctions Induced by the
Nectin–Afadin System 9
3.1. Interaction between the nectin–afadin and
cadherin–catenin systems 9
3.2. Cross-talk between nectin and integrin 11
3.3. Cooperative roles of nectin and integrin
avb3 in intracellular signaling 13
3.4. Regulation of adhesion activity of cadherin by nectin 17
3.5. Roles of nectin and growth factor receptor in cell survival 17
3.6. Disassembly of adherens junctions and
epithelial-to-mesenchymal transition 19
4. Formation of Tight Junctions Regulated by the
Nectin–Afadin System 22
4.1. Components of tight junctions 22
4.2. Integrity of tight junctions mediated by nectin 24
4.3. The nectin and Par complex in the formation of cell polarity
and tight junctions 26
5. Roles of Nectin and Necl-5 27
5.1. Roles of nectin in nectin-mediated cell–cell adhesions 27
5.2. Physiological roles of Necl-5 32
5.3. Pathological implications of nectin and Necl-5 38

Department of Molecular Biology and Biochemistry, Osaka University Graduate School of Medicine/Faculty
of Medicine, Suita, Osaka 565-0871, Japan

International Review of Cytology, Volume 265 # 2008 Elsevier Inc.

ISSN 0074-7696, DOI: 10.1016/S0074-7696(07)65001-3 All rights reserved.

1
2 Hisakazu Ogita and Yoshimi Takai

6. Common Utilization of Signaling Molecules in

Forming Leading Edges and Cell–Cell Adhesion 39
7. Concluding Remarks 40
References 41

Abstract
Integrin, cadherin, and growth factor receptor are key molecules for fundamen-
tal cellular functions including cell movement, proliferation, differentiation,
adhesion, and survival. These cell surface molecules cross-talk with each other
in the regulation of such cellular functions. Nectin and nectin-like molecule
(Necl) have been identified as cell adhesion molecules that belong to the immu-
noglobulin superfamily. Nectin and Necl play important roles in the integration of
integrin, cadherin, and growth factor receptor at the cell–cell adhesion sites of
contacting cells and at the leading edges of moving cells, and thus are also
involved in the fundamental cellular functions together with integrin, cadherin,
and growth factor receptor. This chapter describes how newly identified cell
adhesion molecules, nectin and Necl, modulate the cross-talk among integrin,
cadherin, and growth factor receptor and how these integrated molecules act in
the regulation of fundamental cellular functions.

Key Words: Cadherin, Cell functions, Growth factor receptor, Integrin, Necl,
Nectin. ß 2008 Elsevier Inc.

1. Introduction
Cell movement, proliferation, adhesion, differentiation, and survival
are fundamental cellular functions in multicellular organisms (Gumbiner,
1996; Guo and Hay, 1999; Lauffenburger and Horwitz, 1996; Lin and
Bissell, 1993; Perez-Moreno et al., 2003; Vaux and Korsmeyer, 1999).
Cell adhesion molecules (CAMs) including integrin and cadherin and
growth factor receptors such as platelet-derived growth factor (PDGF)
receptor play pivotal roles in these cellular functions. In addition to these
CAMs and growth factor receptors localized at the surface of cells, a number
of intracellular signaling molecules, which are positively and negatively
controlled by extracellular stimuli through these CAMs and receptors, are
also involved in the regulation of the cellular functions. The roles of CAMs
and receptors and their related intracellular signalings are mutually well
organized to maintain the cellular functions and are thus essential for
living of not only the cells but also multicellular organisms. The disruption
of the organized functions of CAMs and receptors causes the cellular
dysfunction and may lead to pathological, even more life-threatening,
disorders of individuals.
Nectin and Necl in Cellular Functions 3

On the other hand, cell differentiation and survival are directly related to
the cell fate. These phenomena are known to be mainly regulated by the
growth factor-induced signals (Birling and Price, 1995; Pettmann and
Henderson, 1998). However, it has been demonstrated that integrin is
also involved in the differentiation of certain tissues such as the epidermis
(Watt, 2002). Moreover, cell adhesion to the substratum is indispensable for
the survival of cells, and in turn, loss of cell–matrix or cell–cell adhesion
causes cell death by apoptosis or anoikis (Bergin et al., 2000; Fouquet et al.,
2004; Hofmann et al., 2007; Ruoslahti and Reed, 1994). Thus, cell differ-
entiation and survival are also correlated with the relationship between
growth factors and CAMs.
Cultured normal cells move and proliferate until they become confluent
and form cell–cell junctions. After the establishment of cell–cell junctions,
they arrest cell movement and proliferation. This phenomenon was identified
over a half century ago as contact inhibition of cell movement and prolifera-
tion (Abercrombie and Heaysman, 1953; Farquhar and Palade, 1963).
In contrast, transformed cells abnormally continue to move and proliferate
even after they contact each other, and thus contact inhibition of transformed
cells is disrupted, resulting in the enhancement of their invasiveness into
neighboring tissues and metastasis to other organs. Although CAMs and
receptors essentially act in cell movement and proliferation and their contribu-
tions to cell movement and proliferation have been extensively studied for
a long time (Benito and Lorenzo, 1993; Lauffenburger and Horwitz, 1996),
the molecular mechanism for contact inhibition of cell movement and
proliferation has been poorly elucidated to date.
Cell adhesion includes cell–cell and cell–matrix junctions. At cell–matrix
junctions, integrin is a key CAM and comprises heterodimers with a and b
subunits (Geiger et al., 2001). To date, 18 a subunits and 8 b subunits have
been identified and 25 of their combinations were reported (Kinbara et al.,
2003). It is involved in the formation of focal adhesions and focal complexes,
which are specialized subcellular apparatuses including several signaling
molecules that transduce integrin-initiated outside-in signals and also mod-
ulate the affinity of integrin to the extracellular matrix (inside-out signals).
Integrin is also reported to be important for cell movement, proliferation,
and differentiation as well as cell adhesion (Geiger et al., 2001; Kinbara et al.,
2003; Watt, 2002). On the other hand, the molecular mechanism of cell–
cell junctions has been well characterized in epithelial cells. Epithelial cells
contain at least four types of junctional apparatuses: tight junctions (TJs),
adherens junctions (AJs), desmosomes, and gap junctions, all of which
collectively form junctional complexes at the intercellular adhesion sites.
TJs are localized at the most apical side of cell–cell junctions. Two major
functions of TJs are to act as a barrier, preventing the passage of soluble
molecules through the gaps between cells, and as a fence, keeping the cell
surface proteins and lipids in the basolateral region separate from those in the
4 Hisakazu Ogita and Yoshimi Takai

apical region (Tsukita and Furuse, 2002; Tsukita et al., 1999). However, the
fence function of TJs is controversial, because the apical marker proteins and
the basolateral ones are normally distributed on the plasma membrane even
in the epithelial cells in which TJs are completely disrupted (Umeda et al.,
2006). AJs serve as a mechanically adhesive apparatus between neighboring
cells. The functions of AJs and TJs are mainly regulated by several CAMs
and their related peripheral membrane proteins. Claudin, occludin, and
junctional adhesion molecule (JAM) are major Ca2þ-independent CAMs
located at TJs (Tsukita et al., 1999), while at AJs, E-cadherin and nectin are
major Ca2þ-dependent and -independent CAMs, respectively (Takai and
Nakanishi, 2003; Takeichi, 1991). The claudin and cadherin families consist
of a large number of members: more than 20 and 80 members, respectively
(Mitic et al., 2000; Yagi and Takeichi, 2000). The JAM family is also
composed of four members and JAM-like molecule (Ebnet et al., 2004),
but occludin-related genes have not been identified yet (Tsukita et al.,
2001). There is a cross-talk between cell–cell and cell–matrix junctions
and the formations of both types of junctions are mutually regulated
(Pignatelli, 1998; Siu and Cheng, 2004). We mainly describe the features
of AJs and TJs in this chapter. For the concerns on desmosomes and gap
junctions, other excellent reviews would be helpful (Garrod et al., 2002;
Kumar and Gilula, 1996).
Although the molecular mechanisms of the cellular functions including
cell movement, proliferation, adhesion, differentiation, and survival have
been individually studied, the integrated investigation of these cellular
functions is quite important to understand the whole cell architecture.
Moreover, the integrated and harmonized regulation of these cellular
functions is indispensable for living of multicellular organisms. Thus, in
this chapter, we focus on the newly identified CAMs nectin and nectin-like
molecule (Necl), of which the molecular structure is similar to that of
nectin, and describe the molecular mechanism of the cross-talk between
CAMs and growth factor receptors.

2. Molecular and Structural Features of

Nectin and Nectin-Like Molecule
Nectin is a Ca2þ-independent cell–cell adhesion molecule with three
immunoglobulin (Ig)-like loops at its extracellular region, single transmem-
brane segment, and one intracellular region (Takai et al., 2003; Takai and
Nakanishi, 2003) (Fig. 1.1A). To date the nectin family consists of four
members: nectin-1, nectin-2, nectin-3, and nectin-4. The genetic distance
of the nectin and Necl (see later) family members is estimated by construc-
tion of a phylogenetic tree (Fig. 1.1B). Each nectin member has two or
Nectin and Necl in Cellular Functions 5

A
Nectins (-1, -2, -3, -4)

Trans- F-actin-binding
membrane region
S-S S-S S-S
1
479–549 PR(1) PR(2) PR(3)
(Glu/Ala-X-Tyr-Val)

Necls (-1, -2, -3, -4, -5) PDZ

DIL FHA RA(2) RA(1)

Trans-
membrane
S-S S-S S-S
1 389–680

B Nectin-1 C
Necl-5/Tage4 ? ?
(Rodent)
Nectin-3 CD96/ CD226/
Necl-5
Nectin-2 tactile DNAM-1

Nectin-4
Necl-5/PVR/CD155
Nectin-4 Nectin-1 Nectin-3 Nectin-2
(human)

Necl-3 Necl-4

Necl-1 Necl-2 0.1

Necl-1 Necl-2 CRTAM

Figure 1.1 Molecular structures of nectins, Necls, and afadin and their interactions.
(A) Schematic representatives of molecular structures of nectins, Necls, and afadin.
Nectins and Necls both contains three immunoglobulin-like loops in their extracellular
region, one membrane-spanning region, and one cytoplasmic region. Nectin family
members, except nectin-4, possess a consensus motif of four amino acids (E/A-X-Y-V)
for interaction with afadin. Nectin-4 has another C-terminal motif, but also binds afa-
din. Afadin has two Ras-association (RA) domains, a forkhead-associated (FHA)
domain, a DIL domain, a PDZ domain, three proline-rich (PR) domains, and an
F-actin-binding domain. Direct binding between nectins and afadin is conducted
through the C-terminal motif of nectins and the PDZ domain of afadin, which
links nectin to the actin cytoskeleton. (B) Phylogenetic analysis of nectins and Necls.
The nectin and Necl amino acid sequences were aligned using the CLASTALWprogram
and a phylogenetic tree was constructed using tree-drawing software (TreeViewPPC).
Branch lengths are drawn to scale and the longer branches represent more genetic
changes. (C) Homophilic and heterophilic transinteractions among nectins, Necls, and
other immunoglobulin-like molecules. Only known homophilic (looped arrows)
and heterophilic (double arrows) interactions are indicated in this figure.

three alternative splicing isoforms. For nectin-1, there are three isoforms:
nectin-1a, nectin-1b, and nectin-1g; nectin-2 is composed of two isoforms:
nectin-2a and nectin-2d; nectin-3 has three isoforms: nectin-3a, nectin-3b,
and nectin-3g; and nectin-4 also contains two splicing isoforms, whose
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