Intertwined Wdr47-NTD dimer recognizes a basic-helical motif in Camsap proteins for proper central-pair microtubule formation
In: Cell Reports, Jg. 41 (2022-11-01), S. 111589-111589
Online
unknown
Zugriff:
Calmodulin-regulated spectrin-associated proteins (Camsaps) bind to the N-terminal domain of WD40-repeat 47 (Wdr47-NTD; featured with a LisH-CTLH motif) to properly generate axonemal central-pair microtubules (CP-MTs) for the planar beat pattern of mammalian motile multicilia. The underlying molecular mechanism, however, remains unclear. Here, we determine the structures of apo-Wdr47-NTD and Wdr47-NTD in complex with a characteristic Wdr47-binding region (WBR) from Camsap3. Wdr47-NTD forms an intertwined dimer with a special cross-over region (COR) in addition to the canonical LisH and globular α-helical core (GAC). The basic WBR peptide adopts an α-helical conformation and anchors to a tailored acidic pocket embedded in the COR. Mutations in this target-binding pocket disrupt the interaction between Wdr47-NTD and Camsap3. Impairing Wdr47-Camsap interactions markedly reduces rescue effects of Wdr47 on CP-MTs and ciliary beat of Wdr47-deficient ependymal cells. Thus, Wdr47-NTD functions by recognizing a specific basic helical motif in Camsap proteins via its non-canonical COR, a target-binding site in LisH-CTLH-containing domains.
Titel: |
Intertwined Wdr47-NTD dimer recognizes a basic-helical motif in Camsap proteins for proper central-pair microtubule formation
|
---|---|
Autor/in / Beteiligte Person: | Ren, Jinqi ; Li, Dong ; Liu, Juyuan ; Liu, Hao ; Yan, Xiumin ; Zhu, Xueliang ; Feng, Wei |
Link: | |
Zeitschrift: | Cell Reports, Jg. 41 (2022-11-01), S. 111589-111589 |
Veröffentlichung: | Elsevier BV, 2022 |
Medientyp: | unknown |
ISSN: | 2211-1247 (print) |
DOI: | 10.1016/j.celrep.2022.111589 |
Schlagwort: |
|
Sonstiges: |
|