R
Raul Rojas
Researcher at National Institutes of Health
Publications - 12
Citations - 2119
Raul Rojas is an academic researcher from National Institutes of Health. The author has contributed to research in topics: Retromer & Retromer complex. The author has an hindex of 11, co-authored 12 publications receiving 1958 citations. Previous affiliations of Raul Rojas include United States Department of Health and Human Services.
Papers
More filters
Journal ArticleDOI
Retrograde transport from endosomes to the trans-Golgi network.
Juan S. Bonifacino,Raul Rojas +1 more
TL;DR: A central role for a 'tubular endosomal network' in sorting to recycling pathways that lead not only to the trans-Golgi network but also to different plasma-membrane domains and to specialized storage vesicles is proposed.
Journal ArticleDOI
Regulation of retromer recruitment to endosomes by sequential action of Rab5 and Rab7
Raul Rojas,Thijs van Vlijmen,Gonzalo A. Mardones,Yogikala Prabhu,Adriana L. Rojas,Shabaz Mohammed,Albert J. R. Heck,Graça Raposo,Peter van der Sluijs,Juan S. Bonifacino +9 more
TL;DR: It is demonstrated that Rab5 and Rab7 act in concert to regulate retromer recruitment to endosomes.
Journal ArticleDOI
Functional architecture of the retromer cargo-recognition complex.
Aitor Hierro,Adriana L. Rojas,Raul Rojas,Namita Murthy,Gregory Effantin,Andrey V. Kajava,Alasdair C. Steven,Juan S. Bonifacino,James H. Hurley +8 more
TL;DR: In this article, the crystal structure of a VPS29-VPS35 subcomplex was reported, showing how the metallophosphoesterase-fold subunit VPS 29 acts as a scaffold for the carboxy-terminal half of VPS35.
Journal ArticleDOI
Interchangeable but Essential Functions of SNX1 and SNX2 in the Association of Retromer with Endosomes and the Trafficking of Mannose 6-Phosphate Receptors
TL;DR: Biochemical and functional analyses of endogenous retromers in the human cell line HeLa indicate that the mammalian retromer complex assembles by sequential association of SNX1/2 and Vps26-Vps29-VPS35 subcomplexes on endosomal membranes and thatSNX1 and SNX2 play interchangeable but essential roles inretromer structure and function.
Journal ArticleDOI
The retromer subunit Vps26 has an arrestin fold and binds Vps35 through its C-terminal domain
TL;DR: The mammalian retromer complex consists of SNX1, SNX2, VPS26, Vps29 and Vps35, and retrieves lysosomal enzyme receptors from endosomes to the trans-Golgi network and for the function of yeast Vps26 in carboxypeptidase Y sorting.