Cargando…
Phosphorylation of Arp2 is not essential for Arp2/3 complex activity in fission yeast
LeClaire et al presented evidence that phosphorylation of three sites on the Arp2 subunit activates the Arp2/3 complex to nucleate actin filaments. We mutated the homologous residues of Arp2 (Y198, T233, and T234) in the fission yeast genome to amino acids that preclude or mimic phosphorylation. Arp...
Autores principales: | Epstein, Alexander E, Espinoza-Sanchez, Sofia, Pollard, Thomas D |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Life Science Alliance LLC
2018
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6238581/ https://www.ncbi.nlm.nih.gov/pubmed/30456391 http://dx.doi.org/10.26508/lsa.201800202 |
Ejemplares similares
-
Phosphorylation of the Arp2 Subunit Relieves Auto-inhibitory
Interactions for Arp2/3 Complex Activation
por: Narayanan, Arjun, et al.
Publicado: (2011) -
The Nck-interacting kinase NIK increases Arp2/3 complex activity by phosphorylating the Arp2 subunit
por: LeClaire, Lawrence L., et al.
Publicado: (2015) -
Interactions of WASp, myosin-I, and verprolin with Arp2/3 complex during actin patch assembly in fission yeast
por: Sirotkin, Vladimir, et al.
Publicado: (2005) -
Effects of Arp2 and Arp3 nucleotide-binding pocket mutations on Arp2/3 complex function
por: Martin, Adam C., et al.
Publicado: (2005) -
Fission Yeast Myosin-I, Myo1p, Stimulates Actin Assembly by Arp2/3 Complex and Shares Functions with Wasp
por: Lee, Wei-Lih, et al.
Publicado: (2000)