In This Issue - pv

doi:10.1038/nchembio1106-v

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Membranes stay afloat - p559

doi:10.1038/nchembio1106-559

The difficulty in working with lipids and other membrane components has left many fundamental questions about the biochemistry of membranes unanswered. New techniques are required to determine how cell membranes are organized structurally and functionally.

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Phase behavior of lipid mixtures - pp560 - 563

Gerald W Feigenson

doi:10.1038/nchembio1106-560

Biological membranes are two-dimensional mixtures of an enormous number of different components. Modeling cell membranes as simple bilayer mixtures reveals rich phase behavior, but how can we use the observed phase behavior to understand the real membranes?

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The physical chemistry of biological membranes - pp564 - 567

Joshua Zimmerberg & Klaus Gawrisch

doi:10.1038/nchembio1106-564

Physical chemistry explains the principles of self-organization of lipids into bilayers that form the matrix of biological membranes, and continuum theory of membrane energetics is successful in explaining many biological processes. With increasing sophistication of investigative tools, there is now a growing appreciation for lipid diversity and for the role of individual lipids and specific lipid-protein interactions in membrane structure and function.

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Randy Schekman - p568

Mirella Bucci

doi:10.1038/nchembio1106-568

As a pioneer in the field of membrane traffic, Randy Schekman shares a compelling historical perspective on the roles of various disciplines in forming a field and defining a scientist.

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Right on cue - pp569 - 570

Douglas A Lauffenburger

doi:10.1038/nchembio1106-569

Understanding how cytokines interact with multimeric cell receptors to generate signals governing cell behavioral responses is crucial for the development of these promising pharmacological agents. A powerful quantitative approach is reported that was used to analyze the complicated case of binding of the GDNF family member artemin to the heteromeric GFR3-Ret receptor.

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See also: Article by Schlee et al.

S-nitrosylation TRiPs a calcium switch - pp570 - 571

Matthew W Foster, Douglas T Hess & Jonathan S Stamler

doi:10.1038/nchembio1106-570

Accumulating evidence indicates that protein S-nitrosylation may convey a broad spectrum of cellular signals. S-nitrosylation of critical cysteine thiols activates a subset of cation-permeable, transient receptor potential channel proteins (TRPs), which may represent a general mechanism for regulating stimulus-coupled cellular Ca²⁺ flux.

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See also: Article by Yoshida et al.

Flip-flopping salt bridges gate an ion channel - pp572 - 573

Anna Moroni & Gerhard Thiel

doi:10.1038/nchembio1106-572

Ion-channel gating, or stochastic fluctuation between an open and a closed state, is not fully understood at the atomic level. Analysis of the bacterial channel OmpA now suggests that one mode of gating depends on the switching of a salt bridge within the pore.

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See also: Article by Hong et al.

Solving an old puzzle in phospholipid biosynthesis - pp573 - 574

Gustavo E Schujman & Diego de Mendoza

doi:10.1038/nchembio1106-573

A new pathway involving a fatty acid intermediate for the initiation of membrane phospholipid synthesis has been identified. This finding answers the question of how most bacteria catalyze the first acylation step in phosphatidic acid formation.

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Research Highlights - p575

doi:10.1038/nchembio1106-575

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