2008
DOI: 10.1016/j.febslet.2008.06.037
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Flightless‐I, a gelsolin family member and transcriptional regulator, preferentially binds directly to activated cytosolic CaMK‐II

Abstract: In order to evaluate links between Ca 2+ /calmodulin (CaM)-dependent protein kinase type II (CaMK-II) and cell cycle progression, CaMK-II binding partners were sought in proliferating cells by epitope-tag tandem mass spectrometry. One protein identified was the gelsolin family member, flightless-I (Fli-I). Fli-I is not a CaMK-II substrate, but binds directly and preferentially to constitutively active (T 287 D) CaMK-II over inactive CaMK-II. Fli-I gradually enters the nucleus upon CaMK-II inhibition and is ret… Show more

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Cited by 31 publications
(29 citation statements)
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“…Flightless-I has been found to inhibit caspase-1 activation as a pseudosubstrate in a manner similar to CrmA, which contains a caspase-1 substrate recognition sequence and functions as an inhibitory substrate1925. Moreover, Flightless-I has an N-terminal leucine-rich repeat (LRR) protein–protein interaction domain that has many identified binding partners, including LRRFIPs, TRIP and CaMK-II12142930. The connection between LRRFIP2–Flightless-I interaction and Flightless-I-mediated caspase-1 inhibition we reported here have revealed the whole picture of Flightless-I interacting proteins.…”
Section: Discussionmentioning
confidence: 99%
“…Flightless-I has been found to inhibit caspase-1 activation as a pseudosubstrate in a manner similar to CrmA, which contains a caspase-1 substrate recognition sequence and functions as an inhibitory substrate1925. Moreover, Flightless-I has an N-terminal leucine-rich repeat (LRR) protein–protein interaction domain that has many identified binding partners, including LRRFIPs, TRIP and CaMK-II12142930. The connection between LRRFIP2–Flightless-I interaction and Flightless-I-mediated caspase-1 inhibition we reported here have revealed the whole picture of Flightless-I interacting proteins.…”
Section: Discussionmentioning
confidence: 99%
“…Mutations in this gene are either embryonically lethal or lead to the occurrence of degenerated embryos (Kopecki and Cowin, 2008). More importantly, regarding reproductive aspects, FLiI leads to hormonal co-activation of estrogen, which is fundamental for placental development during pregnancy (Seward et al, 2008).…”
Section: Resultsmentioning
confidence: 99%
“…In addition to its role as a regulator of the cytoskeleton, the LRR domain allows Flii to bind a number of other proteins unrelated to actin, including LRR Flii interacting proteins 1 and 2 (LRRFIP1 and LRRFIP2) and the double-stranded RNA-binding protein TAR RNA interacting protein (Wilson et al, 1998;Fong and de Couet, 1999). Flii is also involved in numerous cellular activities including regulating transcription via co-activation of nuclear hormone receptors (Archer et al, 2004;Lee et al, 2004) and regulation of b-catenin-dependent transcription (Lee and Stallcup, 2006), important signaling pathways including the Toll-like receptor pathway (Wang et al, 2006;Dai et al, 2009), cellular polarity, asymmetric cell division (Deng et al, 2007), proliferation via interactions with calmodulin-dependent protein kinase type II (Seward et al, 2008), inflammation, and cytokine production via caspase activation and IL-1b maturation (Li et al, 2008).…”
mentioning
confidence: 99%