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Altogether, these data provide new insight into the central role of ACBD3 in recruiting PI4KB by enterovirus 3A and reveal the minimal domains of ACBD3 involved in recruiting PI4KB and supporting enterovirus replication.
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PI4KIIIbeta interaction with the VHS domain of GGA2 affected PI4KIIIbeta localization.
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several disordered regions of PI4KB become protected from proteolytical degradation upon 14-3-3 binding.
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esults show that Aichi virus 3A protein activates the lipid kinase activity of PI4KIIIb,which activation is sensitized by the protein ACBD3. The interfaces between PI4KIIIbeta-ACBD3 and ACBD3-3A were mapped with hydrogen-deuterium exchange mass spectrometry.
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The results showed that, in contrast to the enteroviruses and the cardioviruses, foot-and-mouth disease virus replication does not require PI4KIII (PI4KIIIalpha and PI4KIIIbeta), and phosphatidylinositol 4-phosphate levels do not increase in foot-and-mouth disease virus-infected cells and phosphatidylinositol 4-phosphate is not seen at replication organelles.
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Data show that ACBD3 can recruit PI4KB to model membranes as well as redirect PI4KB to cellular membranes where it is not naturally found. Also, results show that ACBD3 regulates the enzymatic activity of PI4KB kinase through membrane recruitment rather than allostery.
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Analysis reveals novel aspects of the PI4KIIIb-Rab11 complex and determines binding and catalytic sites of the kinase.
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PI4KIIIbeta likely plays a role in breast oncogenesis and that cooperation between Rab11a and PI4KIIIbeta represents a novel Akt activation pathway.
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Although human rhinovirus 3A protein was previously shown to interact with ACBD3, these data suggest that PI4KIIIbeta recruitment occurred independently of both GBF1 and ACBD3.
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Authors found that NS5A and PI4KB competed for association of acyl-coenzyme A binding domain containing protein 3 (ACBD3), which inhibited hepatitis C virus replication.
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These results suggest that poliovirus proteins modulate PI4KB activity and provide PI4P for recruitment of OSBP to accumulate unesterified cholesterol on virus-induced membrane structure for formation of a virus replication complex.
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Host ACBD3, PI4KIIIBETA and Aichi virus proteins complexes enhances phosphatidylinositol 4-phosphate synthesis and is critical for viral replication.
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these data provide a mechanism for how PI4KIIIbeta coordinates Rab11 and its effectors on PI4P-enriched membranes and also provide strategies for the design of specific inhibitors that could potentially target plasmodial PI4KIIIbeta to combat malaria.
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The lipid kinase PI4KIIIbeta preserves lysosomal identity.
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During authentic HCV infection, PI4P plays an integral role in virus replication; the vesicular transport proteins ARF1 and GBF1 colocalized with PI4KIIIbeta and were both required for HCV replication.
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The 3A protein of picornaviruses utilizes the golgi adaptor protein ACBD3 to recruit PI4KIIIbeta.
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Phosphatidylinositol 4-kinase IIIbeta is required for severe acute respiratory syndrome coronavirus spike-mediated cell entry.
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results indicate that a viral protein/ACBD3/PI4KB complex is formed to synthesize PI4P at the AiV RNA replication sites and plays an essential role in viral RNA replication
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Our data establish PtdIns(4,5)P(2) as a direct activator of TRPV6 and demonstrate that intracellular ATP regulates the channel indirectly as a substrate for type III PI4Ks
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The PI4KIIIbeta likely plays an important role in mammary neoplasia and acinar development.
