15 research outputs found
A study of experimental techniques for prealigning and clamping inertial measurement sensors without major system recalibration
Experimental techniques for prealigning and clamping inertial measurement sensors without major system recalibratio
Development of optimum clamp combinations for strap-down inertial measuring units with field replaceable sensors
Optimum clamp combinations for strap down inertial measuring units with field replaceable sensor
Distribution and biodiversity of Singapore gorgonians (sub-class Octocorallia) - a preliminary survey
10.1007/BF00005658Hydrobiologia2851-3101-109HYDR
Heterogeneous Nuclear Ribonucleoprotein A1 Regulates Cyclin D1 and c-myc Internal Ribosome Entry Site Function through Akt Signaling*S⃞
The translation of the cyclin D1 and c-myc mRNAs occurs via
internal ribosome entry site (IRES)-mediated initiation under conditions of
reduced eIF-4F complex formation and Akt activity. Here we identify hnRNP A1
as an IRES trans-acting factor that regulates cyclin D1 and
c-myc IRES activity, depending on the Akt status of the cell. hnRNP
A1 binds both IRESs in vitro and in intact cells and enhances in
vitro IRES-dependent reporter expression. Akt regulates this IRES
activity by inducing phosphorylation of hnRNP A1 on serine 199. Serine
199-phosphorylated hnRNP A1 binds to the IRESs normally but is unable to
support IRES activity in vitro. Reducing expression levels of hnRNP
A1 or overexpressing a dominant negative version of the protein markedly
inhibits rapamycin-stimulated IRES activity in cells and correlated with
redistribution of cyclin D1 and c-myc transcripts from heavy
polysomes to monosomes. Importantly, knockdown of hnRNP A1 also renders
quiescent Akt-containing cells sensitive to rapamycin-induced G1
arrest. These results support a role for hnRNP A1 in mediating
rapamycin-induced alterations of cyclin D1 and c-myc IRES activity in
an Akt-dependent manner and provide the first direct link between Akt and the
regulation of IRES activity