Matches in SemOpenAlex for { <https://semopenalex.org/work/W4210256768> ?p ?o ?g. }
Showing items 1 to 82 of
82
with 100 items per page.
- W4210256768 endingPage "12" @default.
- W4210256768 startingPage "1" @default.
- W4210256768 abstract "The proteins of the MARCKS (myristoylated alanine-rich C kinase substrate) family were first identified as prominent substrates of protein kinase C (PKC). Since then, these proteins have been implicated in the regulation of brain development and postnatal survival, cellular migration and adhesion, as well as endo-, exo- and phago-cytosis, and neurosecretion. The effector domain of MARCKS proteins is phosphorylated by PKC, binds to calmodulin and contributes to membrane binding. This multitude of mutually exclusive interactions allows cross-talk between the signal transduction pathways involving PKC and calmodulin. This review focuses on recent, mostly biophysical and biochemical results renewing interest in this protein family. MARCKS membrane binding is now understood at the molecular level. From a structural point of view, there is a consensus emerging that MARCKS proteins are ‘natively unfolded'. Interestingly, domains similar to the effector domain have been discovered in other proteins. Furthermore, since the effector domain enhances the polymerization of actin in vitro, MARCKS proteins have been proposed to mediate regulation of the actin cytoskeleton. However, the recent observations that MARCKS might serve to sequester phosphatidylinositol 4,5-bisphosphate in the plasma membrane of unstimulated cells suggest an alternative model for the control of the actin cytoskeleton. While myristoylation is classically considered to be a co-translational, irreversible event, new reports on MARCKS proteins suggest a more dynamic picture of this protein modification. Finally, studies with mice lacking MARCKS proteins have investigated the functions of these proteins during embryonic development in the intact organism." @default.
- W4210256768 created "2022-02-08" @default.
- W4210256768 creator A5036952238 @default.
- W4210256768 creator A5058630619 @default.
- W4210256768 creator A5063664079 @default.
- W4210256768 date "2002-02-08" @default.
- W4210256768 modified "2023-10-14" @default.
- W4210256768 title "Cross-talk unfolded: MARCKS proteins" @default.
- W4210256768 doi "https://doi.org/10.1042/bj3620001" @default.
- W4210256768 hasPublicationYear "2002" @default.
- W4210256768 type Work @default.
- W4210256768 citedByCount "185" @default.
- W4210256768 countsByYear W42102567682012 @default.
- W4210256768 countsByYear W42102567682013 @default.
- W4210256768 countsByYear W42102567682014 @default.
- W4210256768 countsByYear W42102567682015 @default.
- W4210256768 countsByYear W42102567682016 @default.
- W4210256768 countsByYear W42102567682017 @default.
- W4210256768 countsByYear W42102567682018 @default.
- W4210256768 countsByYear W42102567682019 @default.
- W4210256768 countsByYear W42102567682020 @default.
- W4210256768 countsByYear W42102567682021 @default.
- W4210256768 countsByYear W42102567682022 @default.
- W4210256768 countsByYear W42102567682023 @default.
- W4210256768 crossrefType "journal-article" @default.
- W4210256768 hasAuthorship W4210256768A5036952238 @default.
- W4210256768 hasAuthorship W4210256768A5058630619 @default.
- W4210256768 hasAuthorship W4210256768A5063664079 @default.
- W4210256768 hasConcept C11960822 @default.
- W4210256768 hasConcept C125705527 @default.
- W4210256768 hasConcept C142669718 @default.
- W4210256768 hasConcept C144647389 @default.
- W4210256768 hasConcept C1491633281 @default.
- W4210256768 hasConcept C161200384 @default.
- W4210256768 hasConcept C195794163 @default.
- W4210256768 hasConcept C200342125 @default.
- W4210256768 hasConcept C2780780085 @default.
- W4210256768 hasConcept C2993400109 @default.
- W4210256768 hasConcept C41625074 @default.
- W4210256768 hasConcept C51785407 @default.
- W4210256768 hasConcept C55493867 @default.
- W4210256768 hasConcept C62478195 @default.
- W4210256768 hasConcept C77207865 @default.
- W4210256768 hasConcept C86803240 @default.
- W4210256768 hasConcept C95444343 @default.
- W4210256768 hasConceptScore W4210256768C11960822 @default.
- W4210256768 hasConceptScore W4210256768C125705527 @default.
- W4210256768 hasConceptScore W4210256768C142669718 @default.
- W4210256768 hasConceptScore W4210256768C144647389 @default.
- W4210256768 hasConceptScore W4210256768C1491633281 @default.
- W4210256768 hasConceptScore W4210256768C161200384 @default.
- W4210256768 hasConceptScore W4210256768C195794163 @default.
- W4210256768 hasConceptScore W4210256768C200342125 @default.
- W4210256768 hasConceptScore W4210256768C2780780085 @default.
- W4210256768 hasConceptScore W4210256768C2993400109 @default.
- W4210256768 hasConceptScore W4210256768C41625074 @default.
- W4210256768 hasConceptScore W4210256768C51785407 @default.
- W4210256768 hasConceptScore W4210256768C55493867 @default.
- W4210256768 hasConceptScore W4210256768C62478195 @default.
- W4210256768 hasConceptScore W4210256768C77207865 @default.
- W4210256768 hasConceptScore W4210256768C86803240 @default.
- W4210256768 hasConceptScore W4210256768C95444343 @default.
- W4210256768 hasIssue "1" @default.
- W4210256768 hasLocation W42102567681 @default.
- W4210256768 hasOpenAccess W4210256768 @default.
- W4210256768 hasPrimaryLocation W42102567681 @default.
- W4210256768 hasRelatedWork W1972920997 @default.
- W4210256768 hasRelatedWork W2007560959 @default.
- W4210256768 hasRelatedWork W2010774973 @default.
- W4210256768 hasRelatedWork W2037902728 @default.
- W4210256768 hasRelatedWork W2041305500 @default.
- W4210256768 hasRelatedWork W2052929996 @default.
- W4210256768 hasRelatedWork W2070268599 @default.
- W4210256768 hasRelatedWork W21038042 @default.
- W4210256768 hasRelatedWork W2108592410 @default.
- W4210256768 hasRelatedWork W4237404576 @default.
- W4210256768 hasVolume "362" @default.
- W4210256768 isParatext "false" @default.
- W4210256768 isRetracted "false" @default.
- W4210256768 workType "article" @default.