In:
FEBS Letters, Wiley, Vol. 593, No. 11 ( 2019-06), p. 1154-1165
Abstract:
Non‐erythroid spectrin or fodrin is present as part of the γ‐tubulin ring complex (γ‐Tu RC ) in brain tissue and brain derived cells. Here, we show that fodrin, which is otherwise known for providing structural support to the cell membrane, interacts directly with γ‐tubulin within the γ‐Tu RC through a GRIP 2‐like motif. Turbidometric analysis of microtubule polymerization with nucleation‐potent γ‐Tu RC isolated from HEK ‐293 cells that lack fodrin and the γ‐Tu RC from goat brain that contains fodrin shows inefficiency of the latter to promote nucleation. The involvement of fodrin was confirmed by the reduction in the microtubule polymerization efficiency of HEK ‐293 derived γ‐Tu RC s upon addition of purified brain fodrin. Thus, the interaction of fodrin with gamma‐tubulin is responsible for its inhibitory effect on γ‐tubulin mediated microtubule nucleation.
Type of Medium:
Online Resource
ISSN:
0014-5793
,
1873-3468
DOI:
10.1002/feb2.2019.593.issue-11
DOI:
10.1002/1873-3468.13425
Language:
English
Publisher:
Wiley
Publication Date:
2019
detail.hit.zdb_id:
1460391-3
SSG:
12
Permalink