کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
4342270 | 1295861 | 2006 | 9 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Phosphorylation at the hydrophobic site of protein kinase C Apl II is increased during intermediate term facilitation
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کلمات کلیدی
TORPDBuPDK-1Sf9PKCSpodoptera frugiperda5-HT5-hydroxytryptamine (serotonin) - 5-hydroxytryptamine (سروتونین)PI-3 kinase - PI-3 کینازAplysia - آپلیساAutophosphorylation - اتوفسفورلاسیونRapamycin - راپامایسینPhosphatidylserine - فسفاتیدیلسرینphosphoinositide-3 kinase - فسفونیوزیتید-3 کینازphorbol dibutyrate - فوربل dibutyratetarget of rapamycin - هدف از رپامایسینProtein kinase C - پروتئین کیناز سیLearning and memory - یادگیری و حافظه
موضوعات مرتبط
علوم زیستی و بیوفناوری
علم عصب شناسی
علوم اعصاب (عمومی)
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چکیده انگلیسی
In Aplysia, persistent increases in synaptic strength are paralleled by the persistent activation of the novel protein kinase C Apl II. We raised a phosphospecific antibody against serine 725, the hydrophobic motif in protein kinase C Apl II. Phosphorylation of serine 725 increased in parallel to the persistent activation of the kinase. We expressed protein kinase C where this site was mutated to an alanine to prevent phosphorylation. The mutated protein kinase C showed decreased specific activity consistent with a model where the kinase is less stable in the absence of phosphorylation of this site. Endogenous phosphorylation of protein kinase C Apl II at serine 725 was unaffected by either activation of protein kinase C by phorbol esters, or inhibition of protein kinase C using two distinct inhibitors, suggesting the site is not autophosphorylated. Consistent with this, overexpressed kinase-dead protein kinase C Apl II still was phosphorylated at serine 725, although to a lesser extent than wild-type protein kinase C Apl II. While PDK appears to interact with the serine 725 site, it is not responsible for its phosphorylation. Finally inhibition of phosphoinositide-3 kinase or the target of rapamycin by pharmacological agents did not block basal phosphorylation of serine 725 in Aplysia ganglia. Our results suggest trans-phosphorylation of protein kinase C Apl II as Ser 725 occurs during persistent activation of the kinase, but this does not appear to be downstream of phosphoinositide-3 kinase.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Neuroscience - Volume 141, Issue 1, 2006, Pages 277-285
Journal: Neuroscience - Volume 141, Issue 1, 2006, Pages 277-285
نویسندگان
T. Lim, W.S. Sossin,