In This Issue
People & Ideas
ER stress induces expression of miR-708, which suppresses the production of rhodopsin to prevent ER overloading in retinal epithelial cells.
PGL proteins act as scaffolds that recruit RNPs during C. elegans germ granule formation.
Like the nuclear pore complex, FG repeat–containing P-granule proteins interact to help establish a size-exclusion barrier.
The use of new candidate markers for yeast quiescence reveals that quiescence entry and exit primarily rely on cellular metabolic status and can be uncoupled from the cell cycle.
The astrin–kinastrin/SKAP complex localizes to microtubule plus ends and facilitates chromosome alignment
Kinastrin is identified as a major interacting partner for astrin in mitotic cells, and is required for astrin targeting to microtubule plus ends.
A vertebrate N-end rule degron reveals that Orc6 is required in mitosis for daughter cell abscission
In addition to its function as an initiator of DNA replication, vertebrate Orc6 is also required for the final step of cytokinesis.
Association of Akt with phosphatidylserine enhances binding to PIP3, inducing conformational changes in Akt that promote its phosphorylation-mediated activation.
Centrosomal localization of kinase-active CK1δ is required for neurite outgrowth in response to Wnt-3a.
Mapping of fission yeast precursor node interaction modules and assembly reveals important steps in contractile ring assembly.
MKS and NPHP modules cooperate to establish basal body/transition zone membrane associations and ciliary gate function during ciliogenesis
Eight proteins, defects in which are associated with Meckel-Gruber syndrome and nephronophthisis ciliopathies, work together as two functional modules at the transition zone to establish basal body/transition zone connections with the membrane and barricade entry of non-ciliary components into this organelle.
Fzd9, induced upon osteoblast differentiation, is required for bone matrix mineralization in primary osteoblasts.
Intercellular traction forces or lateral alignment of cadherin molecules can influence adherens junction dynamics by altering the cadherin dimerization interface.