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Researchers discover a new mechanism of protein secretion in a pathogenic bacterium.

People & Ideas

Müller initiated the comparative analysis of metabolic pathways in anaerobic eukaryotes.


Elmo–Dock complexes are involved not just in integrin-based adhesions but also in the initial formation of strong cadherin-based adhesions through the regulation of local Rho GTPase activity and actin remodeling.

Redox and Src family kinase signaling in tissue adjacent to a wound coordinates initial attraction of leukocytes and the subsequent repulsion of neutrophils following contact with macrophages to resolve inflammation.


Nuclear BRCA2 is oligomeric and associated with RAD51, possibly sequestering it until it is delivered to DNA damage sites.

A holin (ChiW) and an endopeptidase (ChiX) operate in tandem as components of a protein secretion system used by the gram-negative bacterium Serratia marcescens to secrete the chitinolytic machinery.

CDK5 activates the tumor suppressor DLC1 by phosphorylating and diminishing the binding of an autoinhibitory region of DLC1 to its Rho-GAP domain and allows it to localize to focal adhesions.

PIP2 binds vinculin and directs its oligomerization, which promotes proper focal adhesion structure and function.

In skeletogenic mesenchyme, SOXC proteins enter the APC–Axin destruction complex to inhibit β-catenin phosphorylation by GSK3 and thereby synergize with canonical WNT signaling to inhibit chondrogenesis.


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