Details

Autor(en) / Beteiligte

• Assis, L. H. P.
• Silva-Junior, R. M. P.
• Dolce, L. G.
• Alborghetti, M. R.
• Honorato, R. V.
• Nascimento, A. F. Z.
• Melo-Hanchuk, T. D.
• Trindade, D. M.
• Tonoli, C. C. C.
• Santos, C. T.
• Oliveira, P. S. L.
• Larson, R. E.
• Kobarg, J.
• Espreafico, E. M.
• Giuseppe, P. O.
• Murakami, M. T.

Titel

The molecular motor Myosin Va interacts with the cilia-centrosomal protein RPGRIP1L

Ist Teil von

• Scientific reports, 2017-03, Vol.7 (1), p.43692-43692, Article 43692

Ort / Verlag

London: Nature Publishing Group UK

Erscheinungsjahr

2017

Quelle

Free E-Journal (出版社公開部分のみ）

Beschreibungen/Notizen

• Myosin Va (MyoVa) is an actin-based molecular motor abundantly found at the centrosome. However, the role of MyoVa at this organelle has been elusive due to the lack of evidence on interacting partners or functional data. Herein, we combined yeast two-hybrid screen, biochemical studies and cellular assays to demonstrate that MyoVa interacts with RPGRIP1L, a cilia-centrosomal protein that controls ciliary signaling and positioning. MyoVa binds to the C2 domains of RPGRIP1L via residues located near or in the Rab11a-binding site, a conserved site in the globular tail domain (GTD) from class V myosins. According to proximity ligation assays, MyoVa and RPGRIP1L can interact near the cilium base in ciliated RPE cells. Furthermore, we showed that RPE cells expressing dominant-negative constructs of MyoVa are mostly unciliated, providing the first experimental evidence about a possible link between this molecular motor and cilia-related processes.