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Issues

In This Issue

In Focus

Study suggests that cranial mesenchyme cells must limit Hsp90 secretion during development.

People & Ideas

Biggins studies kinetochores and the mitotic checkpoint.

Review

Evolution

Report

RAD23 proteins facilitate lesion recognition by XPC but then dissociate from the XPC complex and do not participate in the downstream DNA repair process.

The PERK pathway influences the scale of XBP1-mediated gene expression and cell fate in response to ER stress via miR-30c-2*.

Article

Staufen1 interacts with mRNAs with expanded CUG repeats and promotes their nuclear export and translation, while also promoting alternative splicing of other mRNAs.

Both autonomous oxidation and Pdi1p regulate Ero1p’s disulfide bonding–generating activity in response to ER redox levels to optimize oxidative protein folding.

Loss of interaction between the dystonin-a2 isoform and the microtubule-associated protein MAP1B induces microtubule instability and trafficking defects that may underlie certain neuropathies.

An N-terminal BAR-like domain in Num1 mediates its assembly into patches and its interaction with dynein to promote spindle translocation into the mitotic yeast bud.

A minimal mathematical model based on stochastic attachment and detachment of kinetochore microtubules accurately reproduces both normal and abnormal chromosome segregation in fission yeast.

Contrasting with the long-established retrograde model for neurotrophin function, specific immunohistochemical localization of brain-derived neurotrophic factor in the central nervous system supports the alternative model of presynaptic localization and anterograde function.

Hectd1 is a ubiquitin ligase that targets the chaperone Hsp90. In the absence of Hectd1 ubiquitin ligase activity, Hsp90 secretion is elevated, resulting in abnormal behavior of cranial mesenchyme cells.

Tools

In Special Collection: JCB65: Methods

Proximity-dependent biotin identification (BioID) is a new approach making use of biotin ligase fusion proteins for the identification of both interacting and neighboring proteins in their native cellular environment.

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