MISCELLANEA
Two features characterize
Microtubules:
tubule
cellular highways
and
newer
aspects
and
such
as centro-
microtubule
motors.
I
especially liked the coverage of more ‘traditional’ topics such as tubulin
Microtubules
structure, tubulin-drug interactions, tubulin isoforms and non-motor
5. Hyams and Clive
W. Lloyd, Wiley-L&
research. Second, it is well bal-
somes
7 994. $89.95
(439 pages) ISBN 0 477 567 93 2
MAPS. These covered
fields
have
by extensive
long time,
but they
reviews
I found,
for
overlap
be-
a significant
tween the superfamily mediated
chapter on the kinesin and the one on kinesin-
organelle
transport.
Despite these criticisms, Microtubules will certainly be welcomed by people on these cytoskeletal
students or postdocs entering
the field
because
to learn
a
The discoveries
isoforms
the
themselves).
for
exciting
nately, neither the review on tubulin structure nor the chapter on tubulin discusses
modern
structures,
During the past decade, microtubule research has started to blossom again. instability
motors example,
already working
and essential for understanding microtubule behaviour in cells. Unfortu-
of dynamic
more
been
not
remain
covering
topics and especially molecular motors, the book is somewhat redundant (but not as redundant as the
anced between traditional subjects of microtubule biology and biochemistry
constructing
edited by jeremy
chapters
this book.
First, it is quite comprehensive and covers almost all aspects of micro-
question
of
and especially by graduate it will
allow
them
quickly both classical data and the new and exciting developments. Any subject
left uncovered
can be easily
found in current reviews and original articles. The editors of this book have
Vladimir I. Gelfand Dept of Cell and
and motor proteins are just two of many possible examples of recent
post-translational modifications of the tubulin molecule (although a brief
done a great job putting under one cover a long-awaited and compre-
Structural Biology,
advances.
treatment of this can be found under microtubule stabilization). In the
hensive source of information about many aspects of microtubule biology.
Illinois, Urbana,
Keeping
abreast
explosion of new information access to a good reference
of
the
requires covering
University of IL 61801, USA.
the whole field of microtubule research. Microtubules nicely fills the gap between
general textbooks
as Cell Movements
(such initial
by D. Bray) and
sections
cover
tubulin
aspects of microtubules
do not belong
in living cells.
Lymphocyte Activation (Chemical Immunology 59)
Each chapter provides most essential information in its area and refers the reader
to original
edited by L. E. Same/son, (220 pages)
reading.
ISBN 3 8055
in the
and mast
Karger,
with
cytoplasmic
3
of trans-
domains
associated with kinases. These
domains
5976
to the family
membrane receptor tyrosine kinases, but are multimolecular complexes valently tyrosine
1994. DM 251.00/~168.00
articles for further
to
factors to
cell activation p and B cell antigen receptors (TCRs and BCRs) and FceRI]
biochemistry
and genetics, microtubule-associated proteins, and structural and functional
through
early phases of lymphocyte
transduction
these areas. The book’s
activation
of transcription
gene regulatory sequences. The key receptors involved
Translucent
experts actively working in their particular areas of research, and in many cases founded
receptor
the binding
more specialized reviews and original articles. The authors who have contributed to this book are well-known
contain
(tyrosine-based
nonco-
intracellular cytoplasmic
specific
activation
motifs
or antigen
receptor homology motifs) become tyrosine phosphorylated
The tubulin section not only describes the structures of the conven-
that and
tional tubulin molecule and y-tubulin, but also contains reviews on regu-
There have been great advances in the field of signal transduction over the
function as docking sites for members of the Src or ZAP-70/Syk families of
lation
past decade. Particularly
tyrosine classic
of tubulin
synthesis,
tubulin-
specific drugs, genetics of tubulin forms, and dynamics
iso-
of microtubules
been the emergence mon themes
gratifying
has
of some com-
in organisms
as diverse
in vitro. The section on microtubuleassociated proteins contains reviews on most of the ‘conventional’ micro-
as Caenorhabditis elegans, Drosophila and mammals. In these organisms a number of receptors for cell surface
tubule-associated proteins of neural and non-neural origin, as well as chap-
molecules or growth factors have been identified as transmembrane
ters on cytoplasmic and flagellar dyneins
tyrosine
and proteins of the kinesin family. surprisingly,
the final
Not
‘physiological’
section is the most diverse one. Its broad coverage includes microtubule formation in the cell (dynamics of elongation and regulation of centrosome function), plant microtubules, and
microtubule
functions
in
or-
ganelle transport, flagellar motility, and mitosis (kinetochore structure and the role of microtubules in mitosis).
kinases.
Ligand
induces the dimerization
binding
or clustering
of these receptors, leading to the transphosphorylation of their cytoplasmic domains. Enzymes or adapter molecules
dock
onto
the
tyrosine-
kinases. As in the case of the receptor tyrosine kinases,
oligomerization
of TCRs or BCRs leads
to the formation of multimolecular signalling complexes. In this volume, Weissman has written a beautiful review of the multisubunit nalling
TCR complex functions.
and
Peri and
its sigVeillette
describe the tyrosine kinases involved in signalling via the TCR and the CD4 and CD8 coreceptors, while Thomas’ group focuses on tyrosine phosphatases
(CD45,
phosphatases
phosphorylated cytoplasmic tails, forming multimolecular signalling
taining proline-rich sequences phosphatases containing
complexes
domains).
that generate
a number
of
second messengers. Certain distal pathways, particularly the Ras pathway, have been mapped in detail from
TRENDS IN CELL BIOLOGY VOL. 5 MAY 1995
present
conand SH2
De Franc0 and colleagues
a lucid chapter
on the struc-
ture and function of the BCR, and Adamczewski and Kinet describe the
213