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In Focus

Protein family linked to autism suppresses the development of inhibitory synapses.

People & Ideas

Heisenberg is studying how cells’ physical properties drive early developmental events.


Keratin 8 lysine acetylation, which is enhanced by hyperglycemia and reduced by SIRT2, alters filament organization and reduces solubility.

The tumor suppressor APC binds to the intermediate filament vimentin and is required for its microtubule-dependent rearrangements during astrocyte migration.


Structural analysis of a complex of tubulin and tubulin tyrosine ligase (TTL) reveals insights into TTL’s enzymatic mechanism, how it discriminates between α- and β-tubulin, and its possible evolutionary origin.

Myo1 becomes immobile and acts as a scaffold for proteins involved in septum formation and coordination with the actomyosin ring during yeast cytokinesis.

Analysis of three different Rab-RabGEF pairs reveals that RabGEFs contain the minimal targeting machinery for recruiting Rabs to specific membranes.

Phosphorylation of the DYD motif of myosin VI small insert isoform controls the sustainability of exocytosis by tethering secretory granules to the cortical actin network.

Selective suppression of inhibitory synapses—with no effect on excitatory synapses—results from interaction of the autism- and schizophrenia-associated proteins MDGA1 and neuroligin-2 through effects on the neuroligin–neurexin pathway.

Directional neuronal migration is mediated by a dynamic SDF1a source generated through localized SDF1a expression followed by regulated mRNA and protein turnover.



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