Nuclear Envelope Dynamics in Embryos and Somatic Cells

183 Pages·2002·2.956 MB·English

by  Philippe Collas

MOLECULAR BIOLOGY INTELLIGENCE UNIT 23
Philippe Collas
Nuclear Envelope Dynamics
in Embryos and Somatic Cells
M
OLECULAR
B
IOLOGY
I
NTELLIGENCE
U 23
NIT
Nuclear Envelope Dynamics
in Embryos and Somatic Cells
Philippe Collas, Ph.D.
Institute of Medical Biochemistry
University of Oslo
Oslo, Norway
LANDES BIOSCIENCE / EUREKAH.COM KLUWER ACADEMIC / PLENUM PUBLISHERS
GEORGETOWN, TEXAS NEW YORK, NEW YORK
U.S.A U.S.A
NUCLEAR ENVELOPE DYNAMICS IN EMBRYOS AND SOMATIC CELLS
Molecular Biology Intelligence Unit 23
Landes Bioscience / Eurekah.com
and
Kluwer Academic / Plenum Publishers
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Nuclear Envelope Dynamics in Embryos and Somatic Cells edited by Philippe Collas/CRC,
184 pp. 6 x 9/ Landes/Kluwer dual imprint/ Landes series: Molecular Biology Intelligence
Unit 23, ISBN 0-306-47439-5
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CONTENTS
Preface ..................................................................................................ix
1. Dynamics of the Vertebrate Nuclear Envelope.......................................1
Malini Mansharamani, Katherine L. Wilson and James M. Holaska
Abstract.......................................................................................................1
Interphase Nuclear Envelope Structure........................................................1
Nuclear Envelope Disassembly....................................................................3
Nuclear Assembly........................................................................................5
Concluding Remarks...................................................................................8
2. Dynamics of Nuclear Envelope Proteins During the Cell Cycle
in Mammalian Cells.............................................................................15
Jan Ellenberg
Abstract.....................................................................................................15
Why Should Nuclear Envelope Proteins Be Dynamic? ..............................15
What is the Nuclear Envelope Made of?....................................................16
Studying Nuclear Envelope Protein Dynamics ..........................................17
Dynamics in Interphase.............................................................................17
Chromosomes Do not Move Much in Interphase......................................21
Dynamics in Mitosis..................................................................................21
INM Proteins: Switching Retention Off and Back On..............................21
Lamina: Tearing of a Polymer, Dispersion and Re-Import
of Monomers.........................................................................................23
Pore Complex Disassembly and Assembly: Many Open Questions............24
Chromosomes: A Complex Template for Nuclear Assembly......................25
Concluding Remarks.................................................................................25
3. Targeting and Retention of Proteins in the Inner and Pore
Membranes of the Nuclear Envelope....................................................29
Cecilia Östlund, Wei Wu and Howard J. Worman
Abstract.....................................................................................................29
Targeting of Integral Membrane Proteins to the Inner
Nuclear Membrane................................................................................29
Targeting and Retention of Integral Membrane Proteins
to the Pore Membrane...........................................................................35
Targeting of Peripheral Membrane Proteins to the Inner
Nuclear Membrane................................................................................36
Conclusion................................................................................................38
4. Dynamic Connections of Nuclear Envelope Proteins
to Chromatin and the Nuclear Matrix..................................................43
Roland Foisner
Abstract.....................................................................................................43
Introduction..............................................................................................43
Major Components of the Peripheral Nuclear Lamina...............................44
Lamina Proteins in the Nuclear Interior ....................................................46
Interactions at the Interface Between the Lamina
and the Nuclear Scaffold/Chromatin.....................................................47
Potential Functions of Lamina Proteins in Interphase................................49
Dynamics and Functions of Lamina-Chromatin Interactions
During Mitosis......................................................................................50
Conclusions and Future Prospects............................................................53
5. Role of Ran GTPase in Nuclear Envelope Assembly............................61
Chuanmao Zhang and Paul R. Clarke
Abstract.....................................................................................................61
Background...............................................................................................61
Control of Nuclear Envelope Assembly by Ran .........................................64
6. Mitotic Control of Nuclear Pore Complex Assembly...........................73
Khaldon Bodoor and Brian Burke
Introduction..............................................................................................73
The Nuclear Lamina..................................................................................73
The Inner Nuclear Membrane...................................................................73
Nuclear Pore Complexes............................................................................74
Dynamics of the Nuclear Envelope During Mitosis...................................76
Nuclear Envelope Breakdown....................................................................76
Nuclear Envelope Reformation..................................................................77
NPC Assembly ..........................................................................................77
When Does the NPC Become Functional?................................................81
Summary...................................................................................................82
7. Structure, Function and Biogenesis of the Nuclear Envelope
in the Yeast Saccharomyces cerevisiae....................................................87
George Simos
Introduction..............................................................................................87
Overview of the Yeast NPC and its Function in Transport........................88
Composition and Structure-Function Relationships
of the Yeast NPC...................................................................................89
Biogenesis of the Yeast NPCs and Their Role
in the Organization of the NE...............................................................93
Integral Membrane Proteins of the Yeast NE and Their Function.............96
8. Nuclear Envelope Breakdown and Reassembly in C. elegans:
Evolutionary Aspects of Lamina Structure and Function....................103
Yonatan B. Tzur and Yosef Gruenbaum
Abstract...................................................................................................103
The Structure and Protein Composition of the Nuclear Lamina
in C. elegans.........................................................................................103
Possible Functions of the Nuclear Lamina in C. elegans ...........................104
Nuclear Dynamics in C. elegans During Mitosis ......................................106
9. Nuclear Envelope Assembly in Gametes and Pronuclei......................111
D. Poccia, T. Barona, P. Collas and B. Larijani
Abstract...................................................................................................111
Introduction............................................................................................111
Background.............................................................................................111
Sperm Nuclear Envelope Disassembly.....................................................112
Membrane Vesicle Fractions Contributing
to the Nuclear Envelope......................................................................113
Binding of Egg Cytoplasmic Vesicles to Sperm Chromatin
and Nuclear Envelope Remnants.........................................................115
Fusion of Nuclear Envelope Precursor Vesicles........................................117
Completion of Male Pronuclear Envelope Formation..............................123
Comparison with Other Systems and Speculations..................................123
Issues for Future Investigation.................................................................127
10. Nuclear Envelope Dynamics in Drosophila Pronuclear
Formation and in Embryos ................................................................131
Mariana F. Wolfner
Drosophila Nuclear Envelopes..................................................................131
Developmental Changes in Nuclear Envelopes Around
the Time of Fertilization......................................................................132
Conclusion..............................................................................................138
11. The Distribution of Emerin and Lamins in X-Linked
Emery-Dreifuss Muscular Dystrophy.................................................143
G. E. Morris, S. Manilal, I. Holt, D. Tunnah, L. Clements,
F.L. Wilkinson, C.A. Sewry and Nguyen thi Man
Introduction............................................................................................143
A Brief History of EDMD.......................................................................143
The Normal Distribution of Emerin and Lamins ....................................145
Distribution of Emerin and Lamins in X-Linked EDMD........................148
12. Laminopathies: One Gene, Two Proteins, Five Diseases....................153
Corinne Vigouroux and Gisèle Bonne
Abstract...................................................................................................153
Introduction............................................................................................153
Disorders of Cardiac and/or Skeletal Muscles Linked
to LMNA Alterations..........................................................................154
Lipodystrophies and the Familial Partial Lipodystrophy
of the Dunnigan Type (FPLD)............................................................159
Familial Partial Lipodystrophy of the Dunnigan Type (FPLD)................162
Could Some Patients with LMNA Mutations be Affected by Both Skeletal or
Cardiac Muscular Symptoms and Lipodystrophy?...............................163
Experimental Models of Lamin A/C Alterations......................................163
Nuclear Alterations in Cells Harboring LMNA Mutations......................164
Conclusion..............................................................................................166
Addendum...............................................................................................167
Index..................................................................................................173
EDITOR
Philippe Collas, Ph.D.
Institute of Medical Biochemistry
University of Oslo
Oslo, Norway
Chapter 9
CONTRIBUTORS
Teresa Barona Jan Ellenberg
Biology Program Gene Expression and Cell Biology/
University Lusofona Biophysics Programmes
Lisbon, Portugal European Molecular Biology Laboratory
Chapter 9 Heidelberg, Germany
Chapter 2
Khaldon Bodoor
Department of Anatomy and Cell Roland Foisner
Biology Department of Biochemistry and
University of Florida Molecular Cell Biology
Gainesville, Florida, U.S.A. University of Vienna
Chapter 6 Vienna, Austria
Chapter 3
Gisele Bonne
Institut de Myologie Yosef Gruenbaum
INSERM Department of Genetics
Paris, France The Hebrew University of Jerusalem
Chapter 12 Jerusalem, Israel
Chapter 8
Brian Burke
Department of Anatomy and Cell James M. Holaska
Biology Department of Cell Biology and
University of Florida Anatomy,
Gainesville, Florida, U.S.A. Johns Hopkins University School of
Chapter 6 Medicine
Baltimore, Maryland, U.S.A
Paul R. Clarke Chapter 1
Biomedical Research Centre
University of Dundee I. Holt
Dundee, Scotland MRIC Biochemistry Group
Chapter 5 North East Wales Institute
Wrexham, England
L. Clements Chapter 11
MRIC Biochemistry Group
North East Wales Institute
Wrexham, England
Chapter 11
Banafshe Larijani N. thi Man
Cell Biophysics Laboratory MRIC Biochemistry Group
Imperial Cancer Research Fund North East Wales Institute
London, England Wrexham, England
Chapter 9 Chapter 11
S. Manilal
MRIC Biochemistry Group D. Tunnah
North East Wales Institute MRIC Biochemistry Group
Wrexham, England North East Wales Institute
Chapter 11 Wrexham, England
Chapter 11
M. Mansharamani
Department of Cell Biology and Yonatan B. Tzur
Anatomy, Department of Genetics
Johns Hopkins University School of The Hebrew University of Jerusalem
Medicine Jerusalem, Israel
Baltimore, Maryland, U.S.A Chapter 8
Chapter 1
Corinne Vigouroux
G.E. Morris Laboratoire de Biologie Cellulaire
MRIC Biochemistry Group INSERM
North East Wales Institute Paris, France
Wrexham, England Chapter 12
Chapter 11
F.L. Wilkinson
Cecilia Östlund MRIC Biochemistry Group
Department of Medicine North East Wales Institute
Columbia University Wrexham, England
New York, New York, U.S.A. Chapter 11
Chapter 4
K.L. Wilson
Dominic L. Poccia Department of Cell Biology and
Department of Biology Anatomy,
Amherst College Johns Hopkins University School of
Amherst, Massachusetts, U.S.A. Medicine
Chapter 9 Baltimore, Maryland, U.S.A
Chapter 1
C.A. Sewry
MRIC Biochemistry Group Mariana F. Wolfner
North East Wales Institute Department of Molecular Biology and
Wrexham, England Genetics
Chapter 11 Cornell University
Ithaca, New York, U.S.A.
George Simos Chapter 10
Laboratory of Biochemistry
University of Thessaly Howard J. Worman
Larissa, Greece Department of Medicine
Chapter 7 Columbia University
New York, New York, U.S.A.
Chapter 4
Wei Wu Chuanmao Zhang
Department of Medicine Biomedical Research Centre
Columbia University University of Dundee
New York, New York, U.S.A. Dundee, Scotland
Chapter 4 Chapter 5
PREFACE
Roughly twenty-five years of studies of the nuclear envelope have
revealed that it is more than just a bag of membranes enwrapping
chromosomes. The nuclear envelope consists of several domains that
interface the cell cytoplasm and the nucleus: the outer and inner nuclear
membranes, connected by the pore membrane, the nuclear pore complexes
and the filamentous nuclear lamina. Each domain is marked by specific sets
of proteins that mediate interactions with cytoplasmic components (such as
cytoskeletal proteins) or nuclear structures (such as chromosomes). The
nuclear envelope is a highly dynamic structure that reversibly disassembles
when cells divide. How these nuclear envelope domains and proteins are
sorted at mitosis, and how they are targeted back onto chromosomes of the
reforming nuclei in each daughter cell are two fascinating questions that
have dominated the field for many years. Another item which in my mind
makes the field of the nuclear envelope exciting is the range of organisms in
which it has been studied: yeast, sea urchin, star fish, C. elegans, Drosophila,
Xenopus, mammalian cells and more. Each model organism displays com-
mon features in the ways the nuclear envelope breaks down and reforms, but
also pins differences in its organization and dynamics. Another source of
enthusiasm is the variety of experimental systems that have been developed
to investigate the dynamics of the nuclear envelope. These range from cell-
free extracts (again, from eggs or cells of many organisms), to the use of
synthetic beads (which a priori have nothing to do with a nucleus), genetic
studies in C. elegans and recent elaborate 4-D imaging studies in living mam-
malian cells. All these provide unique angles to our view of nuclear envelope
behavior. Finally, for many, the nuclear envelope has experienced a ‘rebirth’
after the identification of mutations in two of its components, the inner
nuclear membrane protein emerin, and nuclear lamins A and C. Mutations
in these proteins are the cause of several forms of dystrophies of skeletal and
cardiac muscles and are life-threatening.
In twelve chapters, prominent experts in their field deliver the latest
views on how molecules and pathways are orchestrated to build, or
disassemble, the nuclear envelope. Each chapter is meant to lead the reader
to a specific domain of the nuclear envelope or to a particular process, whether
this takes place in an egg, an embryo or a somatic—healthy or diseased—cell.
Editing this book would have not been possible without the formidable
contributions from all authors—many thanks to all of them, an initiative
from Ron Landes and the technical support from Cynthia Dworaczyk.
I hope this volume will provide the reader with a better appreciation
of the biology of the nuclear envelope. Have a good time reading it.
Philippe Collas