Nature sub-journal: Palmitoylation is expected to become a new target for anti-cancer drugs

Peripheral membrane proteins can bind to cell membranes through post-translational modifications, such as palmitoylation

To understand how palmitoylation works, scientists at the University of Geneva in Switzerland have developed a new tool that enables observation of this process in living cells

Palmitoylation is the introduction of fatty acids into certain proteins so that they can bind to cell membranes

Co-corresponding author Gonzalo Solis from the Faculty of Medicine of the University of Geneva explains: "In fact, these proteins are produced in the cytoplasm and then 'swim' to the Golgi apparatus, where they are modified and then transported to the place where they function.

Observe and manipulate proteins

To test this hypothesis, the research team led by Professor Vladimir Katanaev of the Faculty of Medicine of the University of Geneva focused on a protein called Gαo, which is normally located in the plasma membrane and in the Golgi apparatus

They used a whole new approach

Vladimir Katanaev and his team developed a tool called SwissKASH to dynamically observe this process under conditions where cells survive

A new drug target

Some peripheral membrane proteins, especially Gα subunit proteins and RAS proteins, are prone to mutation and thus have oncogenic potential

"Inhibiting the enzymes that induce palmitoylation and preventing oncogenic proteins from binding to the plasma membrane is expected to reduce their pathogenicity," noted Gonzalo Solis

Original text retrieval

Solis, GP, Kazemzadeh, A.