In This Issue
People & Ideas
A comprehensive survey of the roles of dynein subunits and adaptors in mitosis reveals that dynein forms distinct complexes requiring specific recruiters and activators to promote orderly progression through mitosis.
A TPR domain–containing N-terminal module of MPS1 is required for its kinetochore localization by Aurora B
The kinetochore localization of MPS1 is necessary for mitotic checkpoint activity and requires the microtubule-binding domain of HEC1 and the Aurora B–dependent regulation of the TPR domain.
Hook1, a microtubule and cargo tethering protein, is important for the sorting of clathrin-independent cargoes away from EEA1+ endosomes and promotes their recycling.
Cycling of the signaling protein phospholipase D through cilia requires the BBSome only for the export phase
The BBSome, a regulator of ciliary membrane protein composition, is required only for the export phase of a process that continuously cycles phospholipase D through cilia.
The MIA complex, composed of FAP100 and FAP73, interacts with I1 dynein components and is required for normal ciliary beat frequency.
Hypoxia increases the levels of ADAM12 in a Notch-dependent manner, leading to increased ectodomain shedding of HB-EGF and subsequent promotion of invadopodia formation.
Ablation of the mTORC2 component rictor in brain or Purkinje cells affects size and neuron morphology
The mTOR complex 2 (mTORC2) is essential in the central nervous system for normal neuronal structure and function, potentially through effects on PKC signaling and independent of the related mTOR complex 1 (mTORC1).
Smooth muscle fascicular reorientation is required for esophageal morphogenesis and dependent on Cdo
Cdo-deficient mice have defects in smooth muscle fascicular reorientation during esophageal morphogenesis, resulting in structural and functional defects including an aberrantly proximal skeletal–smooth muscle boundary and achalasia.
A new immuno-TRAP technique overcomes limitations of spatial resolution and selection bias to identify gene locus associations with a nuclear subcompartment such as promyelocytic leukemia nuclear bodies.
Fluorescent lifetime imaging of an ER-tuned redox-responsive probe revealed an unanticipated stability of ER thiol redox to fluctuations in unfolded protein load, in contrast with sensitivity to lumenal calcium.