PRIMA1
| Proline rich membrane anchor 1 | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||||||
| Symbols | PRIMA1 ; PRIMA | ||||||||||||
| External IDs | OMIM: 613851 MGI: 1926097 HomoloGene: 15783 GeneCards: PRIMA1 Gene | ||||||||||||
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| Orthologs | |||||||||||||
| Species | Human | Mouse | |||||||||||
| Entrez | 145270 | 170952 | |||||||||||
| Ensembl | ENSG00000175785 | ENSMUSG00000041669 | |||||||||||
| UniProt | Q86XR5 | Q810F0 | |||||||||||
| RefSeq (mRNA) | NM_178004 | NM_133364 | |||||||||||
| RefSeq (protein) | NP_821092 | NP_579942 | |||||||||||
| Location (UCSC) |
Chr 14: 93.72 – 93.79 Mb |
Chr 12: 103.2 – 103.24 Mb | |||||||||||
| PubMed search | |||||||||||||
Proline-rich membrane anchor 1, also known as PRiMA, is a protein that in humans is encoded by the PRIMA1 gene.[1][2]
Function
PRiMA functions to organize acetylcholinesterase (AChE) into tetramers, and to anchor AChE at neural cell membranes.[1] This is accomplished by the proline rich anchor domain (PRAD) of PRIMA1 which anchors the tetramer of AChE into the plasma membrane of neural cells and myocytes.[3] The PRAD interacts with the C-terminal T-peptide of AChE.[4]
PRiMA plays a role in targeting AChE to the cell surface and, in neuroblastoma cells, PRiMA the limiting factor of such targeting.[2] In both mice and humans, PRiMA exists as two alternative splice variants that differ in their cytoplasmic regions.
Clinical significance
The severity of neurogenerative diseases, such as Alzheimer’s, can be related to the degradation of AChE.[5]
References
- 1 2 "Entrez Gene: proline rich membrane anchor 1".
- 1 2 Perrier AL, Massoulié J, Krejci E (Jan 2002). "PRiMA: the membrane anchor of acetylcholinesterase in the brain". Neuron 33 (2): 275–85. doi:10.1016/S0896-6273(01)00584-0. PMID 11804574.
- ↑ Xie HQ, Siow NL, Peng HB, Massoulié J, Tsim KW (Dec 2005). "Regulation of PRiMA: membrane anchor of acetylcholinesterase (AChE) in neuron and muscle". Chemico-Biological Interactions. 157-158: 432. doi:10.1016/j.cbi.2005.10.093. PMID 16429581.
- ↑ Perrier NA, Khérif S, Perrier AL, Dumas S, Mallet J, Massoulié J (Oct 2003). "Expression of PRiMA in the mouse brain: membrane anchoring and accumulation of 'tailed' acetylcholinesterase". The European Journal of Neuroscience 18 (7): 1837–47. doi:10.1046/j.1460-9568.2003.02914.x. PMID 14622217.
- ↑ Atack JR, Perry EK, Bonham JR, Perry RH, Tomlinson BE, Blessed G, Fairbairn A (Sep 1983). "Molecular forms of acetylcholinesterase in senile dementia of Alzheimer type: selective loss of the intermediate (10S) form". Neuroscience Letters 40 (2): 199–204. doi:10.1016/0304-3940(83)90302-6. PMID 6633975.
Further reading
- Vanaja DK, Ballman KV, Morlan BW, Cheville JC, Neumann RM, Lieber MM, Tindall DJ, Young CY (Feb 2006). "PDLIM4 repression by hypermethylation as a potential biomarker for prostate cancer". Clinical Cancer Research 12 (4): 1128–36. doi:10.1158/1078-0432.CCR-05-2072. PMID 16489065.
- Bonaldo MF, Lennon G, Soares MB (Sep 1996). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Research 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
- Xie HQ, Choi RC, Leung KW, Chen VP, Chu GK, Tsim KW (Apr 2009). "Transcriptional regulation of proline-rich membrane anchor (PRiMA) of globular form acetylcholinesterase in neuron: an inductive effect of neuron differentiation". Brain Research 1265: 13–23. doi:10.1016/j.brainres.2009.01.065. PMID 19368807.
- Xie HQ, Liang D, Leung KW, Chen VP, Zhu KY, Chan WK, Choi RC, Massoulié J, Tsim KW (Apr 2010). "Targeting acetylcholinesterase to membrane rafts: a function mediated by the proline-rich membrane anchor (PRiMA) in neurons". The Journal of Biological Chemistry 285 (15): 11537–46. doi:10.1074/jbc.M109.038711. PMC 2857032. PMID 20147288.