FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W989860457> ?p ?o ?g. }

• W989860457 abstract "A Ca2+ jelatvitel egyik fontos eleme a plazmamembran Ca2+ATPaz (PMCA), amely az extracellularis terbe tavolit el Ca2+ ionokat. A PMCA egyetlen polipeptidlancbol allo integrans membranfeherje. C-terminalis resze a pumpa aktivitasanak fő szabalyozo regioja. A megfelelő Ca2+ jel kialakitasahoz a PMCA aktivitasanak kozvetlen szabalyozasan tul a PMCA lokalizaciojanak finom szabalyozasara is szukseg van. Eredmenyeink azt bizonyitjak, hogy a PMCA4b izoforma sejten beluli mozgasat a C-terminalisan talalhato osszetett szabalyozasi rendszer befolyasolja: az intracellularis kompartmentek fele iranyito (savanyu regio, internalizacios/retencios) es a feherje plazmamembranba valo kijutasat elősegitő (PDZ-kotő szekvencia) motivumok. A PMCA4b C-terminalisan talalhato PDZ-kotő szekvencia szerepe meghatarozonak bizonyult a PMCA4b plazmamembranon beluli eloszlasanak szempontjabol is. Ehhez kotődve a PSD-95 PDZ-feherje jellegzetes szigetszerű csoportokba rendezi a PMCA4b molekulakat a sejtfelszinen. Ugy talaltuk, hogy specialisan versejtekben es egyeb nem polarizalt sejtekben a PMCA4b-nek lehasad egy rovid, C-terminalis szakasza. A feherje elsődleges szerkezetenek megvaltozasaval atalakul a lokalizaciot szabalyozo rendszer osszetetele. Ennek eredmenyekeppen polarizalt es nem polarizalt sejtekben a PMCA4b varians sejten beluli mozgasa, eloszlasa a plazmamembranban es ezaltal reszvetele a Ca2+ jelatvitelben nagy mertekben kulonbozhet egymastol. | Plasma membrane Ca2+ATPase (PMCA) plays a crucial role in cellular Ca2+ signaling. Its function is to remove excess Ca2+ from the cytosol to the extracellular space. PMCA is an integral membrane protein composed of a single polypeptide chain. It has a special carboxyl terminus that regulates the activity of the pump. In addition, the regulation of the localization of the pump is also crucial for proper Ca2+ signaling. Our results indicate that the intracellular trafficking of the PMCA4b isoform is determined by a complex regulatory mechanism. We found that the C-terminus contains motifs directing the pump to intracellular compartments (acidic cluster and retention/internalization signal) and to the plasma membrane (PDZ-binding sequence). Moreover, the C-terminal PDZ-binding sequence has a significant role in the distribution of the PMCA4b within the plasma membrane. Binding to this motif, a PDZ-domain protein (PSD-95) can arrange the PMCA4b molecules into clusters on the cell surface. We found that in various blood cells and other non-polarized cells a C-terminally truncated PMCA4b is expressed. This modification alters the regulatory system of the C-terminus on the localization of the pump. Therefore the trafficking and plasma membrane distribution of PMCA4b - that may influence the contribution of PMCA4b to Ca2+ signaling' might be considerably different in polarized and non-polarized cells." @default.
• W989860457 created "2016-06-24" @default.
• W989860457 creator A5013447919 @default.
• W989860457 date "2009-01-01" @default.
• W989860457 modified "2023-09-27" @default.
• W989860457 title "A plazmamembrán típusú Ca2+ ATPáz 4b izoforma szerkezetbeli eltérései polarizált és nem-polarizált sejtekben = Distinct structural characteristics of the plasma membrane Ca2+ ATPase 4b forms in polarized and non-polarized cells" @default.
• W989860457 hasPublicationYear "2009" @default.
• W989860457 type Work @default.
• W989860457 sameAs 989860457 @default.
• W989860457 citedByCount "0" @default.
• W989860457 crossrefType "journal-article" @default.
• W989860457 hasAuthorship W989860457A5013447919 @default.
• W989860457 hasConcept C153911025 @default.
• W989860457 hasConcept C154428179 @default.
• W989860457 hasConcept C181199279 @default.
• W989860457 hasConcept C185592680 @default.
• W989860457 hasConcept C23265538 @default.
• W989860457 hasConcept C28406088 @default.
• W989860457 hasConcept C51705589 @default.
• W989860457 hasConcept C55493867 @default.
• W989860457 hasConcept C86803240 @default.
• W989860457 hasConcept C95444343 @default.
• W989860457 hasConcept C98539663 @default.
• W989860457 hasConceptScore W989860457C153911025 @default.
• W989860457 hasConceptScore W989860457C154428179 @default.
• W989860457 hasConceptScore W989860457C181199279 @default.
• W989860457 hasConceptScore W989860457C185592680 @default.
• W989860457 hasConceptScore W989860457C23265538 @default.
• W989860457 hasConceptScore W989860457C28406088 @default.
• W989860457 hasConceptScore W989860457C51705589 @default.
• W989860457 hasConceptScore W989860457C55493867 @default.
• W989860457 hasConceptScore W989860457C86803240 @default.
• W989860457 hasConceptScore W989860457C95444343 @default.
• W989860457 hasConceptScore W989860457C98539663 @default.
• W989860457 hasLocation W9898604571 @default.
• W989860457 hasOpenAccess W989860457 @default.
• W989860457 hasPrimaryLocation W9898604571 @default.
• W989860457 hasRelatedWork W1966227360 @default.
• W989860457 hasRelatedWork W2802273197 @default.
• W989860457 hasRelatedWork W171790020 @default.
• W989860457 isParatext "false" @default.
• W989860457 isRetracted "false" @default.
• W989860457 magId "989860457" @default.
• W989860457 workType "article" @default.