| First Author | Shneidman PS | Year | 1988 |
| Journal | Brain Res | Volume | 464 |
| Issue | 3 | Pages | 217-31 |
| PubMed ID | 3145094 | Mgi Jnum | J:42510 |
| Mgi Id | MGI:1095852 | Doi | 10.1016/0169-328x(88)90028-9 |
| Citation | Shneidman PS, et al. (1988) The structure of the largest murine neurofilament protein (NF-H) as revealed by cDNA and genomic sequences. Brain Res 464(3):217-31 |
| abstractText | The complete primary structure of the largest mammalian neurofilament component, NF-H, is predicted from mouse cDNA and genomic clones, revealing a protein of molecular weight ca. 115,000. A central filament-forming domain structurally typical of all intermediate filament proteins is present, but anomalies are noted which may place constraints on the mechanism of NF-H assembly into filaments. The COOH-terminal portion of the protein is extremely long (661 amino acids) by comparison to non-neuronal intermediate filament components and has a remarkably monotonous, highly charged composition (Glu and Lys at 20% each). Its most remarkable feature is a tandem repeat of a 6 amino acid sequence containing the motif Lys-Ser-Pro that extends for more than half the length of the COOH-terminus. The Lys-Ser-Pro motif appears 48 times and since it is now known that the serine therein is a target for in vivo kinases, the massive axonal phosphorylation of NF-H is explained. Comparison of mouse and human NF-H reveals that otherwise conserved proteins have been subjected to evolutionary mutation within their multiphosphorylation repeat domains, although the Lys-Ser-Pro motif has been conserved. |
