A Survey of Cell Biology [Vol 195] - K. Jeon (AP, 2000) WW

345 Pages·2000·6.04 MB·English

International Review of
A Survey of

Cytology Cell Biology

VOLUME 195

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

Eve Ida Barak
M. Melkonian
Rosa Beddington
Keith E. Mostov
Howard A. Bern
Andreas Oksche
Robert A. Bloodgood
Vladimir R. Pantic´
Dean Bok
Jozef St. Schell
Stanley Cohen
Manfred Schliwa
Rene Couteaux
Robert A. Smith
Marie A. DiBerardino
Wilfred D. Stein
Laurence Etkin
Ralph M. Steinman
Hiroo Fukuda
M. Tazawa
Elizabeth D. Hay
Donald P. Weeks
P. Mark Hogarth
Robin Wright
Anthony P. Mahowald
Alexander L. Yudin
Bruce D. McKee

International Review of
A Survey of

Cytology Cell Biology

Edited by

Kwang W. Jeon

Department of Zoology
The University of Tennessee
Knoxville, Tennessee

VOLUME 195

ACADEMIC PRESS

San Diego
San Francisco
New York
Boston
London
Sydney
Tokyo

CONTENTS

Contributors . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .
vii

Paternal Contributions to the Mammalian Zygote:
Fertilization after Sperm–Egg Fusion

Peter Sutovsky and Gerald Schatten

I.
Introduction . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .
2

II.
Sperm–Oocyte Interactions . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .
2

III.
The Centrosome, Sperm Nucleus, and Pronucleus . . . . . . . . . . . . . . . . . . . . . . . . . . . .
14

IV.
Other Potential Paternal Contributions . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .
28

V.
Concluding Remarks . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .
46

References . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .
47

Coat Proteins Regulating Membrane Traffic

Suzie J. Scales, Marie Gomez, and Thomas E. Kreis

I.
Introduction . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .
67

II.
Clathrin and Adaptor Proteins . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .
69

III.
Coat Proteins . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .
78

IV.
Models for Membrane Traffic in Eukaryotic Cells . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .
96

V.
Regulation of Membrane Traffic through Coat Proteins . . . . . . . . . . . . . . . . . . . . . . . . .
111

VI.
Emerging Families of Coat Proteins . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .
116

VII.
Conclusions and Perspectives . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .
119

References . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .
120

v

vi
CONTENTS

Regulation of Monoamine Receptors in the Brain:
Dynamic Changes during Stress

Gabriele Flu¨gge

I.
Introduction . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .
145

II.
Monoamines . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .
147

III.
Monoamine Receptors . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .
152

IV.
Stress and the Tree Shrew Paradigm . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .
177

V.
Concluding Remarks . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .
193

References . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .
195

Rhodopsin Trafficking and Its Role in Retinal Dystrophies

Ching-Hwa Sung and Andrew W. A. Tai

I.
Introduction . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .
215

II.
The Rod Photoreceptor: A Highly Polarized Cell . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .
216

III.
Rapid Turnover of Rod Disk Membranes . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .
223

IV.
Rhodopsin Trafficking at the Subcellular Level in Normal Rod Photoreceptors . . . . . . .
226

V.
Rhodopsin Trafficking in Pathological Conditions . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .
231

VI.
Molecular Mechanisms of Rhodopsin Trafficking . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .
238

VII.
Rhodopsin Trafficking and Photoreceptor Survival . . . . . . . . . . . . . . . . . . . . . . . . . . . . .
251

VIII.
Concluding Remarks . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .
254

References . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .
255

Calcium Signaling during Abiotic Stress in Plants

Heather Knight

I.
Introduction . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .
269

II.
Low Temperature Stress . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .
271

III.
Osmotic Stress, Drought, and Salinity Stress . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .
283

IV.
Oxidative Stress . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .
290

V.
Anoxia . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .
296

VI.
Heat Stress . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .
299

VII.
Mechanical Stress . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .
301

VIII.
Interactions between Signals . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .
308

IX.
Concluding Remarks . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .
310

References . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .
313

Index . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .
325

CONTRIBUTORS

Numbers in parentheses indicate the pages on which the authors’ contributions begin.

Gabriele Flu¨gge (145), Division of Neurobiology, German Primate Center, 37077 Go¨t-
tingen, Germany

Marie Gomez (67), Howard Hughes Medical Institute, Beckman Center, Department
of Molecular and Cellular Physiology, Stanford University School of Medicine,
Stanford, California 94305

Heather Knight (269), Department of Plant Sciences, University of Oxford, Oxford OXI
3RB, United Kingdom

Thomas E. Kreis (67), Howard Hughes Medical Institute, Beckman Center, Department
of Molecular and Cellular Physiology, Stanford University School of Medicine,
Stanford, California 94305

Suzie J. Scales (67), Howard Hughes Medical Institute, Beckman Center, Department
of Molecular and Cellular Physiology, Stanford University School of Medicine,
Stanford, California 94305

Gerald Schatten(1), Departments ofObstetrics andGynecology, and Celland Develop-
mental Biology, Oregon Health Sciences University, Oregon Regional Primate
Research Center, Beaverton, Oregon 97006

Ching-Hwa Sung (215), Departments of Cell Biology and Anatomy and Ophthalmology,
The Margaret M. Dyson Vision Research Institute, Weill Medical College of
Cornell University, New York, New York 10021

Peter Sutovsky (1), Departments of Obstetrics and Gynecology, and Cell and Develop-
mental Biology, Oregon Health Sciences University, Oregon Regional Primate
Research Center, Beaverton, Oregon 97006

Andrew W. Tai (215), Department of Cell Biology and Anatomy, The Margaret M.
Dyson Vision Research Institute, Weill Medical College of Cornell University,
New York, New York 10021

vii

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Paternal Contributions to the
Mammalian Zygote: Fertilization after
Sperm–Egg Fusion

Peter Sutovsky and Gerald Schatten
Departments of Obstetrics and Gynecology, and Cell and Developmental
Biology, Oregon Health Science University, and the Oregon Regional Primate
Research Center, Beaverton, Oregon 97006

Mammalian fertilization has traditionally been regarded as a simple blending of two
gametes, during which the haploid genome of the fertilizing spermatozoon constitutes the
primary paternal contribution to the resulting embryo. In contrast to this view, new
research provides evidence of important cytoplasmic contributions made by the fertilizing
spermatozoon to the zygotic makeup, to the organization of preimplantation development,
and even reproductive success of new forms of assisted fertilization. The central role of
the sperm-contributed centriole in the reconstitution of zygotic centrosome has been
established in most mammalian species and is put in contrast with strictly maternal
centrosomal inheritance in rodents. The complementary reduction or multiplication of
sperm and oocyte organelles during gametogenesis, exemplified by the differences in the
biogenesis of centrosome in sperm and oocytes, represents an intriguing mechanism for
avoiding their redundancy during early embryogenesis. New studies on perinuclear theca
of sperm revealed its importance for both spermatogenesis and fertilization. Remodeling
of the sperm chromatin into a male pronucleus is guided by oocyte-produced, reducing
peptide glutathione and a number of molecules required for the reconstitution of the
functional nuclear envelope and nuclear skeleton. Although some of the sperm structures
are transformed into zygotic components, the elimination of others is vital to early stages
of embryonic development. Sperm mitochondria, carrying potentially harmful paternal
mtDNA, appear to be eliminated by a ubiquitin-dependent mechanism. Other accessory
structures of the sperm axoneme, including fibrous sheath, microtubule doublets, outer
dense fibers, and the striated columns of connecting piece, are discarded in an orderly
fashion. The new methods of assisted fertilization, represented by intracytoplasmic sperm
injection and round spermatid injection, bypass multiple steps of natural fertilization by
introducing an intact spermatozoon or spermatogenic cell into oocyte cytoplasm.

International Review of Cytology, Vol. 195
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