Regulation of Type III Intermediate Filament Protein Genes in Astrocytes during Development and after Injury

1993 ◽  
pp. 291-302 ◽  
Author(s):  
Monica M. Oblinger ◽  
Susanne A. Kost ◽  
Leelabai D. Singh
Keyword(s):  
Intermediate Filament ◽  
Intermediate Filament Protein ◽  
Type Iii ◽  
Filament Protein

Identification of two N-terminal non-alpha-helical domain motifs important in the assembly of glial fibrillary acidic protein

1994 ◽  
Vol 107 (7) ◽  
pp. 1935-1948 ◽  
Author(s):  
J.E. Ralton ◽  
X. Lu ◽  
A.M. Hutcheson ◽  
R.A. Quinlan
Keyword(s):  
Intermediate Filament ◽  
Consensus Sequence ◽  
Intermediate Filament Protein ◽  
Intermediate Filament Proteins ◽  
Type Iii ◽  
Conserved Sequence ◽  
Terminal Domain ◽  
Filament Assembly ◽  
Arginine Residues ◽  
Filament Protein

The non-alpha-helical N-terminal domain of intermediate filament proteins plays a key role in filament assembly. Previous studies have identified a nonapeptide motif, SSYRRIFGG, in the non-alpha-helical N-terminal domain of vimentin that is required for assembly. This motif is also found in desmin, peripherin and the type IV intermediate filament proteins. GFAP is the only type III intermediate filament protein in which this motif is not readily identified. This study has identified two motifs in the non-alpha-helical N-terminal domain of mouse GFAP that play important roles in GFAP assembly. One motif is located at the very N terminus and has the consensus sequence, MERRRITS-ARRSY. It has some characteristics in common with the vimentin nonapeptide motif, SSYRRIFGG, including its location in the non-alpha-helical N-terminal domain and a concentration of arginine residues. Unlike the vimentin motif in which even conserved sequence changes affect filament assembly, the GFAP consensus sequence, MERRRITS-ARRSY, can be replaced by a completely unrelated sequence; namely, the heptapeptide, MVRANKR, derived from the lambda cII protein. When fused to GFAP sequences with sequential deletions of the N-terminal domain, the lambda cII heptapeptide was used to help identify a second motif, termed the RP-box, which is located just upstream of the GFAP alpha-helical rod domain. This RP-box affected the efficiency of filament assembly as well as protein-protein interactions in the filament, as shown by sedimentation assays and electron microscopy. These results are supported by previous data, which showed that the dramatic reorganization of GFAP within cells was due to phosphorylation-dephosphorylation of a site located in this RP-box. The results in this study suggest the RP-box motif to be a key modulator in the mechanism of GFAP assembly, and support a role for this motif in both the nucleation and elongation phases of filament assembly. The RP-box motif in GFAP has the consensus sequence, RLSL-RM-PP. Sequences similar to the GFAP RP-box motif are also to be found in vimentin, desmin and peripherin. Like GFAP, these include phosphorylation and proteolysis sites and are adjacent to the start of the central alpha-helical rod domain, suggesting that this motif of general importance to type III intermediate filament protein assembly.

Neuronal expression of peripherin, a type III intermediate filament protein, in the mouse hindbrain

2007 ◽  
Vol 128 (6) ◽  
pp. 541-550 ◽  
Author(s):  
Meagan Barclay ◽  
Peter G. Noakes ◽  
Allen F. Ryan ◽  
Jean-Pierre Julien ◽  
Gary D. Housley
Keyword(s):  
Intermediate Filament ◽  
Intermediate Filament Protein ◽  
Type Iii ◽  
Neuronal Expression ◽  
Filament Protein

scholarly journals Phosphorylation of the peripherin 58-kDa neuronal intermediate filament protein

1989 ◽  
Vol 264 (8) ◽  
pp. 4619-4627
Author(s):  
J M Aletta ◽  
M L Shelanski ◽  
L A Greene
Keyword(s):  
Intermediate Filament ◽  
Intermediate Filament Protein ◽  
Filament Protein
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