Matches in SemOpenAlex for { <https://semopenalex.org/work/W2108367997> ?p ?o ?g. }
Showing items 1 to 60 of
60
with 100 items per page.
- W2108367997 abstract "Voltage-gated calcium channels, and L-type calcium channels (LTCs) in particular, provide a key mechanism by which electrical depolarization of a neuron is translated into changes in biochemical signaling systems that alter cellular function and gene expression. Green et al. show that, beyond the acute Ca 2+ -dependent inhibition of LTC conductance by calmodulin, there is an additional mechanism providing a longer-term negative feedback--Ca 2+ -dependent internalization of the channel. The authors modified the LTC Ca v 1.2 with tags in an extracellular loop and on the intracellular N terminus, which allowed them to monitor the fraction of the channel protein that was present on the surface of individual cultured cortical neurons. Electrical depolarization of the neurons decreased the fraction of the channels that was present on the cell surface. Total internal reflection microscopy showed that the channels became internalized in endosomal vesicles. The authors identified a fragment of the channel that produced a dominant-negative inhibition of internalization and, assuming it might be sequestering a protein that regulated the channel, used it in a two-hybrid screen to find an unexpected interacting protein, eIF3e. The eIF3e protein gets its name from its association with the elongation initiation complex, but it also interacts with the proteasome and the COP9 signalosome, complexes that function to degrade or regulate proteins modified by ubiquitination. At least when overexpressed, eIF3e interacted with Ca v 1.2 in cells, and increased amounts of eIF3e were associated with immunoprecipitated Ca v 1.2 when cells had been depolarized. In commentary on the paper, Varela and Zamponi note that a C-terminal fragment of Ca v 1.2 is reported to move to the nucleus and function as a transcription factor. Might eIF3e help route the channel to a compartment where proteolytic release of the C terminus would be activated for control of gene expression? Even if this intriguing scenario does not pan out, it seems likely that alterations in the density of LTCs at the cell surface is a mechanism that will affect a range of physiological processes, from cardiac function to neuronal plasticity. E. M. Green, C. F. Barrett, G. Bultynck, S. M. Shamah, R. E. Dolmetsch, The tumor suppressor eIF3e mediates calcium-dependent internalization of the L-type calcium channel Ca v 1.2. Neuron 55 , 615-632 (2007). [Online Journal] D. Varela, G. W. Zamponi, Use ‘em and lose ‘em--Activity-induced removal of calcium channels from the plasma membrane. Neuron 55 , 539-541 (2007). [Online Journal]" @default.
- W2108367997 created "2016-06-24" @default.
- W2108367997 creator A5011104781 @default.
- W2108367997 date "2007-08-14" @default.
- W2108367997 modified "2023-09-27" @default.
- W2108367997 title "Chillin' Channels Through Internalization" @default.
- W2108367997 doi "https://doi.org/10.1126/stke.4002007tw297" @default.
- W2108367997 hasPublicationYear "2007" @default.
- W2108367997 type Work @default.
- W2108367997 sameAs 2108367997 @default.
- W2108367997 citedByCount "0" @default.
- W2108367997 crossrefType "journal-article" @default.
- W2108367997 hasAuthorship W2108367997A5011104781 @default.
- W2108367997 hasConcept C104317684 @default.
- W2108367997 hasConcept C12554922 @default.
- W2108367997 hasConcept C139770010 @default.
- W2108367997 hasConcept C1491633281 @default.
- W2108367997 hasConcept C181199279 @default.
- W2108367997 hasConcept C185592680 @default.
- W2108367997 hasConcept C201571599 @default.
- W2108367997 hasConcept C28406088 @default.
- W2108367997 hasConcept C29688787 @default.
- W2108367997 hasConcept C4141045 @default.
- W2108367997 hasConcept C55493867 @default.
- W2108367997 hasConcept C71829478 @default.
- W2108367997 hasConcept C79879829 @default.
- W2108367997 hasConcept C86803240 @default.
- W2108367997 hasConcept C95444343 @default.
- W2108367997 hasConceptScore W2108367997C104317684 @default.
- W2108367997 hasConceptScore W2108367997C12554922 @default.
- W2108367997 hasConceptScore W2108367997C139770010 @default.
- W2108367997 hasConceptScore W2108367997C1491633281 @default.
- W2108367997 hasConceptScore W2108367997C181199279 @default.
- W2108367997 hasConceptScore W2108367997C185592680 @default.
- W2108367997 hasConceptScore W2108367997C201571599 @default.
- W2108367997 hasConceptScore W2108367997C28406088 @default.
- W2108367997 hasConceptScore W2108367997C29688787 @default.
- W2108367997 hasConceptScore W2108367997C4141045 @default.
- W2108367997 hasConceptScore W2108367997C55493867 @default.
- W2108367997 hasConceptScore W2108367997C71829478 @default.
- W2108367997 hasConceptScore W2108367997C79879829 @default.
- W2108367997 hasConceptScore W2108367997C86803240 @default.
- W2108367997 hasConceptScore W2108367997C95444343 @default.
- W2108367997 hasLocation W21083679971 @default.
- W2108367997 hasOpenAccess W2108367997 @default.
- W2108367997 hasPrimaryLocation W21083679971 @default.
- W2108367997 hasRelatedWork W1676386679 @default.
- W2108367997 hasRelatedWork W1992216985 @default.
- W2108367997 hasRelatedWork W2004608542 @default.
- W2108367997 hasRelatedWork W2021324087 @default.
- W2108367997 hasRelatedWork W2047085996 @default.
- W2108367997 hasRelatedWork W2081607618 @default.
- W2108367997 hasRelatedWork W2086020659 @default.
- W2108367997 hasRelatedWork W2142925367 @default.
- W2108367997 hasRelatedWork W2152807226 @default.
- W2108367997 hasRelatedWork W3175147527 @default.
- W2108367997 isParatext "false" @default.
- W2108367997 isRetracted "false" @default.
- W2108367997 magId "2108367997" @default.
- W2108367997 workType "article" @default.