Publications de Muhammad Umair Anwar

S-acylation and lipid exchange at the ER-Golgi membrane contact sites regulate pathogen entry in human cells

Cells have evolved endocytic pathways to internalize different molecules, to regulate intra-cellular communication and their interaction with external environment. Pathogens have co-evolved with cells to exploit these processes for infections. In particula ...

EPFL2024

Refining S-acylation: Structure, regulation, dynamics, and therapeutic implications

Françoise Gisou van der Goot Grunberg, Muhammad Umair Anwar

S-acylation is one of the most frequent posttranslational modifications that regulates diverse cellular processes. Anwar and van der Goot discuss the complexity and disease implications of this highly regulated reversible lipidation. ...

Rockefeller University Press2023

ER-Golgi membrane contact sites control the formation of plasma membrane lipid nanodomains

Françoise Gisou van der Goot Grunberg, Laurence Gouzi Abrami, Giovanni D'Angelo, Muhammad Umair Anwar, Oksana Andrei Sergeeva

AMER SOC CELL BIOLOGY2023

ER-Golgi-localized proteins TMED2 and TMED10 control the formation of plasma membrane lipid nanodomains

Françoise Gisou van der Goot Grunberg, Laurence Gouzi Abrami, Giovanni D'Angelo, Laura Capolupo, Francisco De Magalhães Sarmento R De Mesquita, Muhammad Umair Anwar, Oksana Andrei Sergeeva, Audrey Geneviève Chuat, Triana Amen

To promote infections, pathogens exploit host cell machineries such as structural elements of the plasma membrane. Studying these interactions and identifying molecular players are ideal for gaining insights into the fundamental biology of the host cell. H ...

Cell Press - Elsevier2022

Palmitoylated acyl protein thioesterase APT2 deforms membranes to extract substrate acyl chains

Françoise Gisou van der Goot Grunberg, Matteo Dal Peraro, Laurence Gouzi Abrami, Florence Pojer, Maria Josefina Marcaida Lopez, Sylvia Ho, Francisco De Magalhães Sarmento R De Mesquita, Muhammad Umair Anwar, Patrick Alain Sandoz, Martina Audagnotto

Acyl protein thioesterase APT2 interacts with membranes via its charged beta-tongue, becomes palmitoylated by ZDHHC3/7 and deforms the bilayer to extract substrate acyl chains. APT2 deacylation leads to its membrane release and degradation. ...

NATURE RESEARCH2021