Disease relevance of UBQLN2

• Two groups of brain damaged adults, those with cerebrocranial injury (CCI) and victims of cerebrovascular accident (CVA) were tested with the competing sentences test of Willeford (In: Central Auditory Dysfunction. New York: Grune and Stratton, 1977: Chap 2) [1].
• Drs Rigolin and Chap describe a case in which an elderly diabetic man with azotemia survived extreme drug-induced hyperkalemia [2].

High impact information on UBQLN2

• PLIC-1, a newly described ubiquitin-related protein, inhibited both Jurkat migration toward SDF-1alpha and A431 wound healing, but the closely related PLIC-2 did not [3].
• Cyclic hydroxamic-acid-containing peptide 1 (CHAP1), designed as a hybrid of trichostatin A and trapoxin, is a lead compound for the development of potent inhibitors of histone deacetylase (HDAC) [4].
• The ubiquitin-associated domain of hPLIC-2 interacts with the proteasome [5].
• We have shown previously that ADP released upon platelet adhesion mediated by alphaIIb beta3 integrin triggers accumulation of phosphatidylinositol 3',4'-bisphosphate (PtdIns-3,4-P2) (Gironcel, D. , Racaud-Sultan, C., Payrastre, B., Haricot, M., Borchert, G., Kieffer, N., Breton, M., and Chap, H. (1996) FEBS Lett. 389, 253-256) [6].
• We have also compared the S5a binding properties of ubiquitin, SUMO-1, and the ubl domains of hPLIC-2 and hHR23a and have identified the residues on their respective S5a contact surfaces [7].

Biological context of UBQLN2

• Assignment of ubiquilin2 (UBQLN2) to human chromosome xp11. 23-->p11.1 by GeneBridge radiation hybrids [8].
• Chap1 is a duplicated homologue of the yeast Dsk2 gene that is required for transit through the G2/M phase of the cell cycle and expression of the human full-length cDNA restored viability and suppressed the G2/M arrest phenotype of dsk2Delta rad23Delta Saccharomyces cerevisiae mutants [9].
• Deletion of CHAP1 in C. heterostrophus resulted in decreased resistance to oxidative stress caused by hydrogen peroxide and menadione, but the virulence of chap1 mutants was unaffected [10].

Anatomical context of UBQLN2

• Using a fractionation procedure on Percoll gradient (Perret, B., Chap, H. and Douste-Blazy, L. (1979) Biochim. Biophys. Acta 556, 434-446), the enzyme activity displayed the same profile as that of [3H]concanavalin A, a plasma membrane marker [11].

Associations of UBQLN2 with chemical compounds

• These results are discussed in the light of our former hypothesis that arachidonic acid release from platelet phospholipids might occur through the sequential action of a phosphatidylinositol-specific phospholipase C coupled to a diacylglycerol lipase (Mauco, G., Chap, H., Simon, M.F. and Douste-Blazy, L. (1978) Biochimie 60, 553-561) [11].

Regulatory relationships of UBQLN2

• Expression of genes encoding antioxidant proteins was induced in the wild type but not in chap1 mutants [10].

References