Psychiatry related information on RIM11

• It is directly involved in diseases such as cancer (by controlling apoptosis and the levels of beta-catenin and cyclin D1), Alzheimer's disease (tau hyperphosphorylation), and diabetes (as a downstream element of insulin action, GSK-3 regulates glycogen and lipid synthesis) [1].

High impact information on RIM11

• Here we show that the stimulatory effect of yeast Rcn1 involves phosphorylation of a conserved serine residue by Mck1, a member of the GSK-3 family of protein kinases [2].
• GSK-3 kinases enhance calcineurin signaling by phosphorylation of RCNs [2].
• In this report we show that in vivo, in cells grown in a medium promoting vegetative growth with acetate as the sole carbon source (SA medium), Rim11 phosphorylates Ime1, the master transcriptional activator required for entry into the meiotic cycle and for the transcription of early meiosis-specific genes [3].
• We further show that the glucose signal is transmitted through Rim11 [4].
• We further show that this nutrient signal is transmitted to Rim11 and consequently to Ime1 by the cyclic AMP/protein kinase A signal transduction pathway [3].

Biological context of RIM11

• Second, overexpression of RIM11 can suppress an ime1 missense mutation (ime1-L321F) but not an ime1 deletion [5].
• We propose that RIM11 stimulates meiotic gene expression through phosphorylation of IME1 [5].
• Three partially defective rim11 mutations alter residues involved in ATP binding or catalysis, and a completely defective rim11 mutation alters a tyrosine residue that corresponds to the site of an essential phosphorylation for glycogen synthase kinase 3 [5].
• The C-terminal tyrosine-rich region is dispensable for transcriptional activation; rather it renders activation dependent upon starvation and RIM11 [6].
• RIM11 maps near CIN4 on chromosome XIII [7].

Anatomical context of RIM11

• To determine whether GSK-3 is required for meiosis entry, rat stage VIIa seminiferous tubule segments were cultured with selective small-molecule GSK-3 inhibitors [8].
• Tau-4R isolated from yeast lacking mds1 was less phosphorylated and bound more to microtubules than Tau-4R isolated from wild type yeast [9].
• Feedback inhibition on cell wall integrity signaling by Zds1 involves Gsk3 phosphorylation of a cAMP-dependent protein kinase regulatory subunit [10].

Associations of RIM11 with chemical compounds

• An Arabidopsis GSK3/shaggy-like gene that complements yeast salt stress-sensitive mutants is induced by NaCl and abscisic acid [11].
• A computer search reveals significant homology to serine/threonine protein kinases closely related to members of the GSK-3 subfamily [12].
• Characterization of one of these mutants, mds1, revealed that it was sensitive not only to novobiocin but also to a wide range of drugs [13].

Physical interactions of RIM11

• Here, we characterize mutant Ime1p derivatives that interact with Rim11p but are not phosphorylated in vitro [14].

Enzymatic interactions of RIM11

• In addition, HA-RIM11 immune complexes phosphorylate a functional IME1 derivative but not the corresponding ime1-L321F derivative [5].
• Rim11p phosphorylates transcription factors Ume6p (unscheduled meiotic gene expression) and Ime1p (inducer of meiosis) to induce meiosis entry [8].

Other interactions of RIM11

• Analysis of RIM11, a yeast protein kinase that phosphorylates the meiotic activator IME1 [5].
• Rog1 binds directly to Rsp5, and their interaction is dependent on GSK-3 [15].
• The 42-kDa tyrosine-phosphorylated protein was identified as Mck1, which is a member of the GSK3 family of protein kinases and previously known to be phosphorylated on tyrosine [16].
• Interaction of yeast repressor-activator protein Ume6p with glycogen synthase kinase 3 homolog Rim11p [17].
• Human Tau was readily phosphorylated at pathological epitopes, but in opposite directions regulated by kinases Mds1 and Pho85, orthologues of glycogen synthase kinase-3beta and cdk5, respectively (1) [9].

Analytical, diagnostic and therapeutic context of RIM11

• We describe here a rapid and efficient method for the purification of GSK-3 by affinity chromatography on an immobilized fragment of axin [1].

References