| First Author | Palmer DN | Year | 2015 |
| Journal | Biochim Biophys Acta | Volume | 1852 |
| Issue | 10 Pt B | Pages | 2287-91 |
| PubMed ID | 26093153 | Mgi Jnum | J:253940 |
| Mgi Id | MGI:6100117 | Doi | 10.1016/j.bbadis.2015.06.014 |
| Citation | Palmer DN (2015) The relevance of the storage of subunit c of ATP synthase in different forms and models of Batten disease (NCLs). Biochim Biophys Acta 1852(10 Pt B):2287-91 |
| abstractText | The discoveries of specific protein storage in the NCLs, particularly of subunit c of ATP synthase in most, and the sphingolipid activator proteins, SAPs or saposins A and D in CLN1, CLN10 and an unassigned form are reviewed. The subunit c stored in the relevant NCLs is the complete mature molecule including an unusual modification found only in animal species, trimethylation of its lysine-43. Because of its strongly hydrophobic and lipid-like properties subunit c is easily overlooked or incorrectly described. This is becoming more of a problem as subunit c is not detected in standard proteomic investigations. Methods are reviewed that allow its unequivocal characterisation. Subunit c storage and cellular storage body accumulation do not cause the neuropathology characteristic of these diseases. The function of the trimethyl group on lysine-43 of subunit c is considered, along with some indications of where its normal turnover may be disrupted in the NCLs. |
