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ProteinЦLipid Interactions. From Membrane Domains to Cellular Networks. Edited by Lukas K. Tamm

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understanding to us, and their book
should make many students enthusiastic
about thermodynamics.
To bring classical thermodynamics
to life in such an appealingly vivid, yet
also mathematically rigorous way, is an
accomplishment that makes this book
highly recommendable.
Marc-Olivier Coppens
Physical Chemistry & Molecular
Delft University of Technology
(The Netherlands)
Protein–Lipid Interactions
From Membrane
Domains to Cellular Networks.
Edited by Lukas K.
Tamm. Wiley-VCH,
Weinheim 2005.
472 pp., hardcover
E 149.00.—ISBN
In this book, Lukas K. Tamm of the
University of Virginia (Charlottesville,
USA) has compiled a collection of
articles that presents a very interesting
and up-to-date overview of the subject
of lipid–protein interactions. Although
the structure of lipid membranes was
correctly described, in principle, several
decades ago, the topic has again become
a focus of scientific interest in the last
few years, especially in discussions about
membrane domains and the heterogeneity that results from their presence.
This heterogeneity affects membrane
proteins, their functions, and their roles
in complex processes such as photosynthesis and signal transduction.
Such processes depend on the interactions between the lipid components
and the proteins within a membrane,
and these interactions are discussed in
detail in the book. It consists of 17 articles, written by scientists who are recognized experts in their special fields,
and these are arranged in six parts
devoted to different topic areas.
Although every article can be read independently of the rest, it is clear that they
are intended to complement each other.
The first part, “How lipids shape proteins”, consists of four articles that are
concerned with the insertion, folding, and
stability of membrane proteins, beginning
with a helices, and continuing through bglobular (barrel-shaped) proteins, such as
OmpA, to bacteriorhodopsin. The fourth
article of this part considers the question
of how mutations of transmembrane
proteins can affect changes in folding
after their insertion.
The second part, “How proteins
shape lipids”, consists of two articles
that describe how X-ray crystallography
and NMR spectroscopy can provide
information about the spatial arrangement and bonding specificity of surfactant molecules and lipids on transmembrane proteins.
The three articles that form the third
part of the book discuss the latest
knowledge in the area of pore-forming
toxins. Special attention is given to poreforming colicins, and to the class of
actinoporins, which are a family of powerful pore-forming proteins found in sea
anemones. Another area in which there
is still much research activity is that of
antimicrobial peptides such as magainins.
The molecular conditions needed for
toxins to show a specific antimicrobial
activity are discussed in detail, as also are
the mechanisms by which membrane
permeability is increased.
The fourth part is concerned with
aspects of membrane fusion. The first of
the three articles begins by discussing
cell fusion during the development of
organisms, with the emphasis on studies
of Drosophila and C. elegans. Here the
main interest is focused not on molecular aspects but on looking at these
processes from a phenomenological
viewpoint, with the help of electron
microscopy. The article is also concerned with cell fusion mediated by
viruses. The latter theme is also taken
up by the editor of the book and his coauthors in the second article, but here
the emphasis is on the molecular structure of viral fusion peptides and fusion
proteins and their interaction with lipids
during the fusion process. The third
article discusses current knowledge
about the fusion processes that form a
part of the secretion transport process in
: 2006 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim
eukaryotic cells, with particular emphasis on the SNARE proteins.
Any up-to-date discussion about
lipid membranes and lipid–protein interactions must include the topic of membrane domains. Here it is treated in the
fifth part of the book under the title
“Cholesterol, lipid rafts, and protein
sorting”. The first of the two articles
discusses protein–lipid interactions specifically in connection with membrane
domains. The article is critical, but at the
same time very informative. The second
article reviews research on the distribution of lipids and proteins in model
membranes, and gives a brief description of the various techniques that are
available for investigating membrane
The sixth and last part consists of
three articles about protein domains
that are responsible for the recruiting of
proteins in cellular membranes. The first
article discusses recent results on reversible bonding by membrane-binding protein domains such as C1, C2, PH, FYVE,
domains. The second article concentrates
specifically on the C2 domains, and
discusses the molecular interaction with
the membrane surface in detail. This
section ends with an article on the
structural mechanisms involved in allosteric regulation of membrane-binding
domains, which nicely complements the
material in the other two articles.
Considered as a whole, this is an
excellent collection of highly topical
articles in the field of lipid–protein
interactions. Every article contains a
comprehensive and up-to-date list of
references, giving the reader access to a
wealth of primary literature. An especially
valuable resource is the compilation of
current data relating to the individual
topics that have been extracted from
protein data banks; these also provide a
good basis for planning further work. The
keyword index enables the reader to find
relevant discussions in the various articles.
The book is a worthwhile addition to the
private collections of all those who are
concerned with lipid–protein interactions.
Andreas Janshoff
Institut f5r Physikalische Chemie
Johannes-Gutenberg-Universit8t Mainz
DOI: 10.1002/anie.200585349
Angew. Chem. Int. Ed. 2006, 45, 1183 – 1184
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interactions, domain, proteinцlipid, luka, tamm, network, edited, membranes, cellular
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