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A high-density genetic interaction map reveals a complex that organizes the mitochondrial inner membrane.

People & Ideas

Akhmanova studies microtubule plus end–binding proteins and proteins that interact with microtubule motors.




A new tool to probe the FG repeat network of the nuclear pore complex transport channel in vivo provides insight into the organization and functional features of the channel.

High-resolution particle tracking shows a specific role for the dynein regulatory factor LIS1 in high-load axonal transport of large vesicles but no evidence for mechanical activation of opposite-directed motors.


Btn1 controls endosome–Golgi retrograde sorting by regulating SNARE phosphorylation and assembly.

Differential expression and activity of the cellular energy regulators GAPDH and NDPK underlie reactive oxygen species–induced damage in the mouse liver and may contribute to human liver disease progression.

The PP2A subunit Twins and the SV40 small T antigen, a functional mimic of Twins, counteract Plk4 autophosphorylation, leading to its stabilization and to subsequent centriole amplification.

The FERM domain–containing protein Lulu2 and p114RhoGEF function at epithelial cell–cell junctions to regulate the actomyosin belt that determines cell shape.

To promote cell survival, the antiapoptotic factor Bcl-xL both inhibits Bax-induced mitochondrial outer membrane permeabilization and stabilizes mitochondrial inner membrane ion flux and thus overall mitochondrial energetic capacity.

In the absence of the pro-apoptotic factor Bim, caspase-8 plays an important role in restraining autoimmunity by inducing cell death in T cells.

Spatial competition between glial cells causes them to partition neuromuscular junctions into discrete domains within a synapse.

MKP-1 limits p38 MAPK signaling in macrophages to promote the resolution of the inflammatory response and tissue repair in muscle through an AKT-dependent mechanism.


In Special Collection: JCB65: Mitochondria

Statement MITO-MAP, a high-density genetic interaction map in budding yeast, identifies a mitochondrial inner membrane–associated complex that promotes normal mitochondrial membrane organization and morphology.


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