ArticlePloS one2013
Fodrin in centrosomes: implication of a role of fodrin in the transport of gamma-tubulin complex in brain.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 10 citations in OpenAlex.
- Calpains as Potential Regulators of Microtubule-Associated Cytokinesis: A Cross-Eukaryotic Unifying Hypothesis.Life (Basel, Switzerland) · 2026Article
- The centrosomal recruitment of γ-tubulin and its microtubule nucleation activity is α-fodrin guided.Cell cycle (Georgetown, Tex.) · 2023Article
- Expression of the human herpesvirus 6A latency-associated transcript U94A impairs cytoskeletal functions in human neural cells.Molecular and cellular neurosciences · 2022Article
- α-Fodrin in Cytoskeletal Organization and the Activity of Certain Key Microtubule Kinesins.Genes · 2021Article
- A Fresh Look at the Structure, Regulation, and Functions of Fodrin.Molecular and cellular biology · 2020Review
- CRISPR/Cas9-Mediated Integration of Large Transgene into PigG3 (Bethesda, Md.) · 2020Article
- α-Fodrin is required for the organization of functional microtubules during mitosis.Cell cycle (Georgetown, Tex.) · 2019Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Gamma-tubulin is the major protein involved in the nucleation of microtubules from centrosomes in eukaryotic cells. It is present in both cytoplasm and centrosome. However, before centrosome maturation prior to mitosis, gamma-tubulin concentration increases dramatically in the centrosome, the mechanism of which is not known. Earlier it was reported that cytoplasmic gamma-tubulin complex isolated from goat brain contains non-erythroid spectrin/fodrin. The major role of erythroid spectrin is to help in the membrane organisation and integrity. However, fodrin or non-erythroid spectrin has a distinct pattern of localisation in brain cells and evidently some special functions over its erythroid counterpart. In this study, we show that fodrin and γ-tubulin are present together in both the cytoplasm and centrosomes in all brain cells except differentiated neurons and astrocytes. Immunoprecipitation studies in purified centrosomes from brain tissue and brain cell lines confirm that fodrin and γ-tubulin interact with each other in centrosomes. Fodrin dissociates from centrosome just after the onset of mitosis, when the concentration of γ-tubulin attains a maximum at centrosomes. Further it is observed that the interaction between fodrin and γ-tubulin in the centrosome is dependent on actin as depolymerisation of microfilaments stops fodrin localization. Image analysis revealed that γ-tubulin concentration also decreased drastically in the centrosome under this condition. This indicates towards a role of fodrin as a regulatory transporter of γ-tubulin to the centrosomes for normal progression of mitosis.
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