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beta-Arrestin 1 and 2 similarly influence mu-opioid receptor mobility and distinctly modulate adenylyl cyclase activity

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11310%2F21%3A10437984" target="_blank" >RIV/00216208:11310/21:10437984 - isvavai.cz</a>

  • Result on the web

    <a href="https://verso.is.cuni.cz/pub/verso.fpl?fname=obd_publikace_handle&handle=~hA_EU~8CL" target="_blank" >https://verso.is.cuni.cz/pub/verso.fpl?fname=obd_publikace_handle&handle=~hA_EU~8CL</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1016/j.cellsig.2021.110124" target="_blank" >10.1016/j.cellsig.2021.110124</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    beta-Arrestin 1 and 2 similarly influence mu-opioid receptor mobility and distinctly modulate adenylyl cyclase activity

  • Original language description

    beta-Arrestins are known to play a crucial role in GPCR-mediated transmembrane signaling processes. However, there are still many unanswered questions, especially those concerning the presumed similarities and differences of beta-arrestin isoforms. Here, we examined the roles of beta-arrestin 1 and beta-arrestin 2 at different levels of mu-opioid receptor (MOR)-regulated signaling, including MOR mobility, internalization of MORs, and adenylyl cyclase (AC) activity. For this purpose, naive HEK293 cells or HEK293 cells stably expressing YFP-tagged MOR were transfected with appropriate siRNAs to block in a specific way the expression of beta-arrestin 1 or beta-arrestin 2. We did not find any significant differences in the ability of beta-arrestin isoforms to influence the lateral mobility of MORs in the plasma membrane. Using FRAP and line-scan FCS, we observed that knockdown of both beta-arrestins similarly increased MOR lateral mobility and diminished the ability of DAMGO and endomorphin-2, respectively, to enhance and slow down receptor diffusion kinetics. However, beta-arrestin 1 and beta-arrestin 2 diversely affected the process of agonist-induced MOR endocytosis and exhibited distinct modulatory effects on AC function. Knockdown of beta-arrestin 1, in contrast to beta-arrestin 2, more effectively suppressed forskolin-stimulated AC activity and prevented the ability of activated-MORs to inhibit the enzyme activity. Moreover, we have demonstrated for the first time that beta-arrestin 1, and partially beta-arrestin 2, may somehow interact with AC and that this interaction is strongly supported by the enzyme activation. These data provide new insights into the functioning of beta-arrestin isoforms and their distinct roles in GPCR-mediated signaling.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • OECD FORD branch

    30105 - Physiology (including cytology)

Result continuities

  • Project

    Result was created during the realization of more than one project. More information in the Projects tab.

  • Continuities

    P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>S - Specificky vyzkum na vysokych skolach

Others

  • Publication year

    2021

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    Cellular Signalling

  • ISSN

    0898-6568

  • e-ISSN

  • Volume of the periodical

    87

  • Issue of the periodical within the volume

    November

  • Country of publishing house

    US - UNITED STATES

  • Number of pages

    10

  • Pages from-to

    110124

  • UT code for WoS article

    000702705800008

  • EID of the result in the Scopus database

    2-s2.0-85113786021