2023
DOI: 10.1002/2211-5463.13700
|View full text |Cite
|
Sign up to set email alerts
|

Effects of truncations in the N‐ and C‐terminal domains of filensin on filament formation with phakinin in cell‐free conditions and cultured cells

Moe Tashiro,
Akari Nakamura,
Yamato Kuratani
et al.

Abstract: Filensin and phakinin are lens fiber cell‐specific proteins that constitute the beaded filaments that are critical for maintaining lens transparency. In the Shumiya cataract rat, filensin 94 kDa undergoes N‐ and C‐terminal proteolytic processing to give a transient 50 kDa fragment and a final 38 kDa fragment, just before opacification. To characterize effects of this processing on filensin function, recombinant proteins representing the two filensin fragments, termed Fil(30‐416) and Fil(30‐369), respectively, … Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
1

Citation Types

0
1
0

Year Published

2024
2024
2024
2024

Publication Types

Select...
2

Relationship

0
2

Authors

Journals

citations
Cited by 2 publications
(1 citation statement)
references
References 76 publications
(169 reference statements)
0
1
0
Order By: Relevance
“…The head-to-tail association involves an "overlap" of the highly conserved rod domain, and interactions with the head domain are vital for dimer formation, probably through electrostatic interactions [16,47]. Finally, in the exceptional case of type VI IFs, it seems that the tail domain of filensin is necessary for beaded filament formation with the naturally tailless phakinin [48,49], while the partial truncation of the N-terminal domain of filensin does not affect filament formation [49].…”
Section: The Role Of Head and Tail Domains In If Assemblymentioning
confidence: 99%
“…The head-to-tail association involves an "overlap" of the highly conserved rod domain, and interactions with the head domain are vital for dimer formation, probably through electrostatic interactions [16,47]. Finally, in the exceptional case of type VI IFs, it seems that the tail domain of filensin is necessary for beaded filament formation with the naturally tailless phakinin [48,49], while the partial truncation of the N-terminal domain of filensin does not affect filament formation [49].…”
Section: The Role Of Head and Tail Domains In If Assemblymentioning
confidence: 99%