PRiMA functions to organize acetylcholinesterase (AChE) into tetramers, and to anchor AChE at neural cell membranes.[4] 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.[6] The PRAD interacts with the C-terminal T-peptide of AChE.[7]
PRiMA plays a role in targeting AChE to the cell surface and, in neuroblastoma cells, PRiMA the limiting factor of such targeting.[5] In both mice and humans, PRiMA exists as two alternative splice variants that differ in their cytoplasmic regions.
^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. Bibcode:2005CBI...157..432X. doi:10.1016/j.cbi.2005.10.093. PMID16429581.
^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. PMID14622217. S2CID21808922.
^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. PMID6633975. S2CID45149066.
