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Gene Review:

Glrp1 - glutamine repeat protein 1

Mus musculus

Synonyms: GRP-1

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Disease relevance of Glrp1

Huntington's disease (HD) is an inherited neurodegenerative disease caused by a glutamine repeat expansion in huntingtin protein [1].
To investigate if GAPDH might interact with other glutamine repeat-containing proteins involved in neurodegenerative disorders, we tested its binding to the androgen receptor which is mutated in spinobulbar muscular atrophy [2].

Psychiatry related information on Glrp1

Huntington disease (HD) is caused by expansion of a glutamine repeat in the amino-terminal region of huntingtin [3].

High impact information on Glrp1

Bassoon, a novel zinc-finger CAG/glutamine-repeat protein selectively localized at the active zone of presynaptic nerve terminals [4].
Huntington's disease (HD) is an inherited, neurodegenerative disorder caused by the expansion of a glutamine repeat in the N-terminus of the huntingtin protein [5].
Aggregation of expanded polyglutamine is thought to be a common pathological mechanism in HD and other glutamine repeat diseases [6].
Characterization of an expanded glutamine repeat androgen receptor in a neuronal cell culture system [7].
In both models, diffuse neuronal nuclear staining and nuclear inclusion bodies are observed in animals expressing the expanded glutamine repeat protein, further implicating the nucleus as a primary site of neuronal dysfunction [8].

Biological context of Glrp1

We found that AR-induced transcriptional activation gradually decreased with increasing glutamine repeat numbers, and polyglutamine expansion caused a specific reduction in transcription activity in motor neurons [9].

Associations of Glrp1 with chemical compounds

Curcumin also causes rapid proteasomal malfunction in the mutant huntingtin expressing cells in comparison with normal glutamine repeat expressing cells [10].

References

Transcriptional Repression of PGC-1alpha by Mutant Huntingtin Leads to Mitochondrial Dysfunction and Neurodegeneration. Cui, L., Jeong, H., Borovecki, F., Parkhurst, C.N., Tanese, N., Krainc, D. Cell (2006) [Pubmed]
Spinocerebellar ataxia type-1 and spinobulbar muscular atrophy gene products interact with glyceraldehyde-3-phosphate dehydrogenase. Koshy, B., Matilla, T., Burright, E.N., Merry, D.E., Fischbeck, K.H., Orr, H.T., Zoghbi, H.Y. Hum. Mol. Genet. (1996) [Pubmed]
Amino-terminal fragments of mutant huntingtin show selective accumulation in striatal neurons and synaptic toxicity. Li, H., Li, S.H., Johnston, H., Shelbourne, P.F., Li, X.J. Nat. Genet. (2000) [Pubmed]
Bassoon, a novel zinc-finger CAG/glutamine-repeat protein selectively localized at the active zone of presynaptic nerve terminals. tom Dieck, S., Sanmartí-Vila, L., Langnaese, K., Richter, K., Kindler, S., Soyke, A., Wex, H., Smalla, K.H., Kämpf, U., Fränzer, J.T., Stumm, M., Garner, C.C., Gundelfinger, E.D. J. Cell Biol. (1998) [Pubmed]
Intranuclear inclusions and neuritic aggregates in transgenic mice expressing a mutant N-terminal fragment of huntingtin. Schilling, G., Becher, M.W., Sharp, A.H., Jinnah, H.A., Duan, K., Kotzuk, J.A., Slunt, H.H., Ratovitski, T., Cooper, J.K., Jenkins, N.A., Copeland, N.G., Price, D.L., Ross, C.A., Borchelt, D.R. Hum. Mol. Genet. (1999) [Pubmed]
Aggregation of N-terminal huntingtin is dependent on the length of its glutamine repeats. Li, S.H., Li, X.J. Hum. Mol. Genet. (1998) [Pubmed]
Characterization of an expanded glutamine repeat androgen receptor in a neuronal cell culture system. Brooks, B.P., Paulson, H.L., Merry, D.E., Salazar-Grueso, E.F., Brinkmann, A.O., Wilson, E.M., Fischbeck, K.H. Neurobiol. Dis. (1997) [Pubmed]
Polyglutamine pathogenesis. Ross, C.A., Wood, J.D., Schilling, G., Peters, M.F., Nucifora, F.C., Cooper, J.K., Sharp, A.H., Margolis, R.L., Borchelt, D.R. Philos. Trans. R. Soc. Lond., B, Biol. Sci. (1999) [Pubmed]
Transcriptional activation by the androgen receptor in X-linked spinal and bulbar muscular atrophy. Nakajima, H., Kimura, F., Nakagawa, T., Furutama, D., Shinoda, K., Shimizu, A., Ohsawa, N. J. Neurol. Sci. (1996) [Pubmed]
Curcumin enhances the polyglutamine-expanded truncated N-terminal huntingtin-induced cell death by promoting proteasomal malfunction. Dikshit, P., Goswami, A., Mishra, A., Nukina, N., Jana, N.R. Biochem. Biophys. Res. Commun. (2006) [Pubmed]

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