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Studying CENP-A nucleosome assembly in a cell-free system defines the role of existing CENP-A nucleosomes in centromere maintenance.
The primary activity of GMFβ in vivo is actin branch disassembly (and not inhibition of Arp2/3 activation), and this activity plays an important role in lamellipodial dynamics and directional migration toward ECM cues.
Both N- and C-terminal microtubule (MT)-binding domains of CENP-F can follow depolymerizing MT ends while bearing a significant load, and the N-terminal domain prefers binding to curled oligomers of tubulin relative to MT walls by approximately fivefold, suggesting that CENP-F may play a role in the firm bonds that form between kinetochores and the flared plus ends of dynamic MTs.
In response to mating pheromone, the yeast MFA2 mRNA is transported to the tip of the mating projection as an RNP granule and translated; integrity of the granules is required for normal mRNA transport and for the mating process.
Kar1 interacts with the C-terminal (CT) region of Sfi1 to tether the yeast centrosome’s bridge to the nuclear envelope; Sfi1-CT and C-terminal Cdc31-binding regions form the antiparallel Sfi1 overlap in the bridge.
Binding of STIL activates Plk4, and the subsequent phosphorylation of STIL by Plk4 primes the binding of STIL to SAS6 to promote centriole assembly.
P2X4 and calmodulin form a signaling complex in late endosomes and lysosomes that promotes fusion and vacuolation in a Ca2+-dependent fashion.
A novel method called kinase-interacting substrate screening based on affinity beads coated with the kinase of interest identifies phosphorylation sites for Rho-kinase and others, which reveals that Rho-kinase substrate Scrib plays a crucial role in the regulation of subcellular contractility by assembling with Rho-kinase and Shroom2.