FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2011056720> ?p ?o ?g. }

• W2011056720 endingPage "25811" @default.
• W2011056720 startingPage "25797" @default.
• W2011056720 abstract "Phosphodiesterases (PDEs) play key roles in cAMP compartmentalization, which is required for intracellular signaling processes, through specific subcellular targeting. Previously, we showed that the long and short forms of Aplysia PDE4 (ApPDE4), which are localized to the membranes of distinct subcellular organelles, play key roles in 5-hydroxytryptamine-induced synaptic facilitation in Aplysia sensory and motor synapses. However, the molecular mechanism of the isoform-specific distinct membrane targeting was not clear. In this study, we further investigated the molecular mechanism of the membrane targeting of the ApPDE4 long and short forms. We found that the membrane targeting of the long form was mediated by hydrophobic interactions, mainly via 16 amino acids at the N-terminal region, whereas the short form was targeted solely to the plasma membrane, mainly by nonspecific electrostatic interactions between their N termini and the negatively charged lipids such as the phosphatidylinositol polyphosphates PI4P and PI(4,5)P2, which are embedded in the inner leaflet of the plasma membrane. Moreover, oligomerization of the long or short form by interaction of their respective upstream conserved region domains, UCR1 and UCR2, enhanced their plasma membrane targeting. These results suggest that the long and short forms of ApPDE4 are distinctly targeted to intracellular membranes through their direct association with the membranes via hydrophobic and electrostatic interactions, respectively. Phosphodiesterases (PDEs) play key roles in cAMP compartmentalization, which is required for intracellular signaling processes, through specific subcellular targeting. Previously, we showed that the long and short forms of Aplysia PDE4 (ApPDE4), which are localized to the membranes of distinct subcellular organelles, play key roles in 5-hydroxytryptamine-induced synaptic facilitation in Aplysia sensory and motor synapses. However, the molecular mechanism of the isoform-specific distinct membrane targeting was not clear. In this study, we further investigated the molecular mechanism of the membrane targeting of the ApPDE4 long and short forms. We found that the membrane targeting of the long form was mediated by hydrophobic interactions, mainly via 16 amino acids at the N-terminal region, whereas the short form was targeted solely to the plasma membrane, mainly by nonspecific electrostatic interactions between their N termini and the negatively charged lipids such as the phosphatidylinositol polyphosphates PI4P and PI(4,5)P2, which are embedded in the inner leaflet of the plasma membrane. Moreover, oligomerization of the long or short form by interaction of their respective upstream conserved region domains, UCR1 and UCR2, enhanced their plasma membrane targeting. These results suggest that the long and short forms of ApPDE4 are distinctly targeted to intracellular membranes through their direct association with the membranes via hydrophobic and electrostatic interactions, respectively." @default.
• W2011056720 created "2016-06-24" @default.
• W2011056720 creator A5009735236 @default.
• W2011056720 creator A5044558421 @default.
• W2011056720 creator A5051414465 @default.
• W2011056720 creator A5054490917 @default.
• W2011056720 creator A5065045333 @default.
• W2011056720 creator A5077180850 @default.
• W2011056720 creator A5082813043 @default.
• W2011056720 creator A5090020843 @default.
• W2011056720 creator A5090060451 @default.
• W2011056720 date "2014-09-01" @default.
• W2011056720 modified "2023-10-03" @default.
• W2011056720 title "Intracellular Membrane Association of the Aplysia cAMP Phosphodiesterase Long and Short Forms via Different Targeting Mechanisms" @default.
• W2011056720 cites W1776649101 @default.
• W2011056720 cites W1857741797 @default.
• W2011056720 cites W1963851797 @default.
• W2011056720 cites W1968946845 @default.
• W2011056720 cites W1971095698 @default.
• W2011056720 cites W1972608995 @default.
• W2011056720 cites W1976344568 @default.
• W2011056720 cites W1986827801 @default.
• W2011056720 cites W1988214498 @default.
• W2011056720 cites W1994337546 @default.
• W2011056720 cites W1997784032 @default.
• W2011056720 cites W2006705808 @default.
• W2011056720 cites W2007513923 @default.
• W2011056720 cites W2017621078 @default.
• W2011056720 cites W2017832480 @default.
• W2011056720 cites W2018012667 @default.
• W2011056720 cites W2026896701 @default.
• W2011056720 cites W2043312574 @default.
• W2011056720 cites W2046138985 @default.
• W2011056720 cites W2046210627 @default.
• W2011056720 cites W2046754637 @default.
• W2011056720 cites W2053964608 @default.
• W2011056720 cites W2054799935 @default.
• W2011056720 cites W2055659589 @default.
• W2011056720 cites W2062453540 @default.
• W2011056720 cites W2062574001 @default.
• W2011056720 cites W2067738389 @default.
• W2011056720 cites W2069644684 @default.
• W2011056720 cites W2070412886 @default.
• W2011056720 cites W2074422008 @default.
• W2011056720 cites W2075634772 @default.
• W2011056720 cites W2082688327 @default.
• W2011056720 cites W2084783054 @default.
• W2011056720 cites W2085035388 @default.
• W2011056720 cites W2087181092 @default.
• W2011056720 cites W2090469070 @default.
• W2011056720 cites W2091701502 @default.
• W2011056720 cites W2091884933 @default.
• W2011056720 cites W2094068658 @default.
• W2011056720 cites W2095071736 @default.
• W2011056720 cites W2109640441 @default.
• W2011056720 cites W2113807807 @default.
• W2011056720 cites W2122218917 @default.
• W2011056720 cites W2123066014 @default.
• W2011056720 cites W2159610000 @default.
• W2011056720 cites W2160979292 @default.
• W2011056720 cites W2301214492 @default.
• W2011056720 cites W4238609105 @default.
• W2011056720 cites W4254104742 @default.
• W2011056720 doi "https://doi.org/10.1074/jbc.m114.572222" @default.
• W2011056720 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4162181" @default.
• W2011056720 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/25077971" @default.
• W2011056720 hasPublicationYear "2014" @default.
• W2011056720 type Work @default.
• W2011056720 sameAs 2011056720 @default.
• W2011056720 citedByCount "18" @default.
• W2011056720 countsByYear W20110567202015 @default.
• W2011056720 countsByYear W20110567202016 @default.
• W2011056720 countsByYear W20110567202017 @default.
• W2011056720 countsByYear W20110567202019 @default.
• W2011056720 countsByYear W20110567202022 @default.
• W2011056720 crossrefType "journal-article" @default.
• W2011056720 hasAuthorship W2011056720A5009735236 @default.
• W2011056720 hasAuthorship W2011056720A5044558421 @default.
• W2011056720 hasAuthorship W2011056720A5051414465 @default.
• W2011056720 hasAuthorship W2011056720A5054490917 @default.
• W2011056720 hasAuthorship W2011056720A5065045333 @default.
• W2011056720 hasAuthorship W2011056720A5077180850 @default.
• W2011056720 hasAuthorship W2011056720A5082813043 @default.
• W2011056720 hasAuthorship W2011056720A5090020843 @default.
• W2011056720 hasAuthorship W2011056720A5090060451 @default.
• W2011056720 hasBestOaLocation W20110567201 @default.
• W2011056720 hasConcept C110455231 @default.
• W2011056720 hasConcept C168240541 @default.
• W2011056720 hasConcept C169760540 @default.
• W2011056720 hasConcept C181199279 @default.
• W2011056720 hasConcept C185592680 @default.
• W2011056720 hasConcept C2778178740 @default.
• W2011056720 hasConcept C41625074 @default.
• W2011056720 hasConcept C55493867 @default.
• W2011056720 hasConcept C62826618 @default.
• W2011056720 hasConcept C79879829 @default.
• W2011056720 hasConcept C86803240 @default.
• W2011056720 hasConcept C95444343 @default.

• next