Phosphorylation of threonine 156 of the μ2 subunit of the AP2 complex is essential for endocytosis in vitro and in vivo

By O. Olusanya, P. D. Andrews, Jason R. Swedlow, E. Smythe. 2001

149 citations recorded by the source corpus.

Subfields: Cell Biology, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/e682405691397f77eac70c827e528beb87a62f47

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Cell Biology

1. E. Smythe
2. M. Robinson
3. K. Ayscough

In Molecular Biology

1. E. Smythe
2. M. Robinson
3. Marcus J. Taylor
4. K. Ayscough

Citations in the corpus

• Functional Analysis of AP-2 α and μ2 Subunits (2006, result): “Our study also agrees with an article by Olusanya et al. (2001) on the role of 2 phosphorylation in vivo, in which tagged wild-type or T156A 2 were transiently transfected into cells.”
• The Ark1/Prk1 family of protein kinases (2003, background): “…has been shown to be an in vitro phosphorylation site (Pauloin & Thurieau, 1993). µ2 phosphorylation has been shown to be important for endocytosis (Olusanya et al., 2001) as the sequestration of the cargo molecule transferrin into newly formed coated pits is inhibited if µ2 phosphorylation is…”