N. Johnsson

Transient septin sumoylation steers a Fir1-Skt5 protein complex between the split septin ring

The paper investigates how septin sumoylation directs the movement of the Fir1-Skt5 complex during yeast cell separation.

The concerted action of SEPT9 and EPLIN modulates the adhesion and migration of human fibroblasts

This study shows that SEPT9 and EPLIN interact to regulate fibroblast adhesion and migration through actin cytoskeleton organization.

Biochemical characterization of a human septin octamer

This study characterizes the biochemical properties of a human septin octamer, showing its polymerization behavior and unique GTP hydrolysis dynamics.

A time resolved interaction analysis of Bem1 reconstructs the flow of Cdc42 during polar growth

The paper maps Bem1's protein interactions in time and space to understand its role in Cdc42 gradient formation during yeast cell cycle stages.

Cdc24, the source of active Cdc42, transiently interacts with septins to create a positive feedback between septin assembly and bud site formation in yeast cells.

The paper shows that Cdc24 interacts with septins to reinforce bud site formation through a positive feedback loop in yeast cells.

An actin nucleation complex catalyzes filament formation at sites of exocytosis

This study shows that Boi1/2 recruit nucleation factors to form actin filaments at exocytosis sites, facilitating vesicle docking and movement in yeast.

YFR016c/Aip5 is part of an actin nucleation complex in budding yeast cells

The paper identifies YFR016c/Aip5 as a novel subunit of the polarisome complex that binds to Bud6 and Spa2 to support actin filament formation at sites of polar growth in yeast cells.

An interaction network of the human SEPT9 established by quantitative mass spectrometry reveals an interplay with myosin motors

The paper identifies SEPT9's interaction network using quantitative proteomics, revealing its role in vesicle transport and actin stress fiber attachment.

The Cell Polarity Proteins Boi1p And Boi2p Stimulate Vesicle Fusion At The Plasma Membrane Of Yeast Cells

The paper identifies Boi1p and Boi2p as essential proteins that mediate vesicle fusion and Cdc42p activation during yeast polar growth.