Results 71 to 80 of about 573,078 (335)

Structural basis of protein phosphatase 2A stable latency [PDF]

open access: yesNature Communications, 2013
The catalytic subunit of protein phosphatase 2A (PP2Ac) is stabilized in a latent form by α4, a regulatory protein essential for cell survival and biogenesis of all PP2A complexes. Here we report the structure of α4 bound to the N-terminal fragment of PP2Ac.
Jiang, Li   +7 more
openaire   +2 more sources

Reciprocal control of viral infection and phosphoinositide dynamics

open access: yesFEBS Letters, EarlyView.
Phosphoinositides, although scarce, regulate key cellular processes, including membrane dynamics and signaling. Viruses exploit these lipids to support their entry, replication, assembly, and egress. The central role of phosphoinositides in infection highlights phosphoinositide metabolism as a promising antiviral target.
Marie Déborah Bancilhon, Bruno Mesmin
wiley   +1 more source

Protein Phosphatase 2A (PP2A) Regulates EG5 to Control Mitotic Progression

open access: yesScientific Reports, 2017
EG5 (KIF11) is a member of the kinesin-like protein family involved in centrosome separation and bipolar spindle formation. When a cell enters mitosis, CDK1 phosphorylates EG5 at Thr926 and promotes EG5 localization on the mitotic spindle which drives ...
Yang Liu   +9 more
doaj   +1 more source

The cytoplasmic adaptor protein Caskin mediates Lar signal transduction during Drosophila motor axon guidance [PDF]

open access: yes, 2011
The multiprotein complexes that receive and transmit axon pathfinding cues during development are essential to circuit generation. Here, we identify and characterize the Drosophila sterile α-motif (SAM) domain-containing protein Caskin, which shares ...
Broihier, Heather T   +3 more
core   +2 more sources

Phosphatidylinositol 4‐kinase as a target of pathogens—friend or foe?

open access: yesFEBS Letters, EarlyView.
This graphical summary illustrates the roles of phosphatidylinositol 4‐kinases (PI4Ks). PI4Ks regulate key cellular processes and can be hijacked by pathogens, such as viruses, bacteria and parasites, to support their intracellular replication. Their dual role as essential host enzymes and pathogen cofactors makes them promising drug targets.
Ana C. Mendes   +3 more
wiley   +1 more source

The effects of protein phosphatase inhibitors on the duration of central sensitization of rat dorsal horn neurons following injection of capsaicin

open access: yesMolecular Pain, 2006
Protein kinases and phosphatases catalyze opposing reactions of phosphorylation and dephosphorylation, which may modulate the function of crucial signaling proteins in central nervous system.
Fang Li   +3 more
doaj   +1 more source

Protein Phosphatase 2A in Lipopolysaccharide-Induced Cyclooxygenase-2 Expression in Murine Lymphatic Endothelial Cells. [PDF]

open access: yesPLoS ONE, 2015
The lymphatic endothelium plays an important role in the maintenance of tissue fluid homeostasis. It also participates in the pathogenesis of several inflammatory diseases.
Yu-Fan Chuang   +6 more
doaj   +1 more source

How to halve ploidy : lessons from budding yeast meiosis [PDF]

open access: yes, 2012
Maintenance of ploidy in sexually reproducing organisms requires a specialized form of cell division called meiosis that generates genetically diverse haploid gametes from diploid germ cells.
Arumugam, Prakash   +2 more
core   +1 more source

B56δ-related protein phosphatase 2A dysfunction identified in patients with intellectual disability.

open access: yesJournal of Clinical Investigation, 2015
Here we report inherited dysregulation of protein phosphatase activity as a cause of intellectual disability (ID). De novo missense mutations in 2 subunits of serine/threonine (Ser/Thr) protein phosphatase 2A (PP2A) were identified in 16 individuals with
G. Houge   +27 more
semanticscholar   +1 more source

Disordered but rhythmic—the role of intrinsic protein disorder in eukaryotic circadian timing

open access: yesFEBS Letters, EarlyView.
Unstructured domains known as intrinsically disordered regions (IDRs) are present in nearly every part of the eukaryotic core circadian oscillator. IDRs enable many diverse inter‐ and intramolecular interactions that support clock function. IDR conformations are highly tunable by post‐translational modifications and environmental conditions, which ...
Emery T. Usher, Jacqueline F. Pelham
wiley   +1 more source

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