کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
4341987 | 1295852 | 2008 | 9 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Post-synaptic density-93 mediates tyrosine-phosphorylation of the N-methyl-d-aspartate receptors
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کلمات کلیدی
SDSSrc family tyrosine kinasesPP2SFKsNR2ANR2BPDZPKCPSD-95N-methyl-d-aspartateNMDAPMSFDMEMPSD4β-phorbol 12-myristate 13-acetate - 4β-فروبل 12-مریستات 13-استاتDMSO - DMSODulbecco's modified Eagle Medium - Eagle Medium اصلاح شده Dulbeccomembrane-associated guanylate kinase - guanylate kinase مرتبط با غشاءMAGUK - آنهاSDS–polyacrylamide gel electrophoresis - الکتروفورز ژل SDS-polyacrylamide gelSDS-PAGE - الکتروفورز ژل پلی آکریل آمیدPost-synaptic density - تراکم پسا سیناپسیlong-term potentiation - تقویت درازمدتLTP - تقویت طولانی مدت یا LTP Dimethylsulfoxide - دیمتیل سولفواکسیدsodium dodecyl sulfate - سدیم دودسیل سولفاتSAP - شیرهphenylmethylsulfonyl fluoride - فنیل متیل سولفونیل فلورایدFyn - فیونknockout - ناکاوتwild-type - نوع وحشیsynapse-associated protein - پروتئین مرتبط با سیناپسProtein kinase C - پروتئین کیناز سی
موضوعات مرتبط
علوم زیستی و بیوفناوری
علم عصب شناسی
علوم اعصاب (عمومی)
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چکیده انگلیسی
Src family protein kinases (SFKs) -mediated tyrosine-phosphorylation regulates N-methyl-d-aspartate (NMDA) receptor synaptic function. Some members of the membrane-associated guanylate kinase (MAGUK) family of proteins bind to both SFKs and NMDA receptors, but it is unclear whether the MAGUK family of proteins is required for SFKs-mediated tyrosine-phosphorylation of the NMDA receptors. Here, we showed by co-immunoprecipitation that post-synaptic density (PSD) -93, a member of the MAGUK family of proteins, interacts with the NMDA receptor subunits NR2A and NR2B as well as with Fyn, a member of the SFKs, in mouse cerebral cortex. Using a biochemical fractionation approach to isolate subcellular compartments revealed that the expression of Fyn, but not of other members of the SFKs (Lyn, Src, and Yes), was significantly decreased in synaptosomal membrane fractions derived from the cerebral cortex of PSD-93 knockout mice. Interestingly, we found that PSD-93 disruption causes reduction of tyrosine-phosphorylated NR2A and NR2B in the same fraction. Moreover, PSD-93 deletion markedly blocked the SFKs-mediated increase in tyrosine-phosphorylated NR2A and NR2B through the protein kinase C pathway after induction with 4-phorbol 12-myristate 13-acetate in cultured cortical neurons. Our findings indicate that PSD-93 appears to mediate tyrosine-phosphorylation of the NMDA receptors and synaptic localization of Fyn.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Neuroscience - Volume 153, Issue 3, 15 May 2008, Pages 700-708
Journal: Neuroscience - Volume 153, Issue 3, 15 May 2008, Pages 700-708
نویسندگان
Y. Sato, Y.-X. Tao, Q. Su, R.A. Johns,