Luciana Renna

Crossing the divide--transport between the endoplasmic reticulum and Golgi apparatus in plants.

Identification and characterization of AtCASP, a plant transmembrane Golgi matrix protein.

Diacidic motifs influence the export of transmembrane proteins from the endoplasmic reticulum in plant cells.

In tobacco leaf epidermal cells, the integrity of protein export from the endoplasmic reticulum and of ER export sites depends on active COPI machinery.

ARL1 plays a role in the binding of the GRIP domain of a peripheral matrix protein to the Golgi apparatus in plant cells.

Multiple roles of ADP-ribosylation factor 1 in plant cells include spatially regulated recruitment of coatomer and elements of the Golgi matrix.

De novo formation of plant endoplasmic reticulum export sites is membrane cargo induced and signal mediated.

A missense mutation in the vacuolar protein GOLD36 causes organizational defects in the ER and aberrant protein trafficking in the plant secretory pathway.

COPII-mediated traffic in plants.

AGD5 is a GTPase-activating protein at the trans-Golgi network.

Evidence for the involvement of the Arabidopsis SEC24A in male transmission.

In Arabidopsis, the spatial and dynamic organization of the endoplasmic reticulum and Golgi apparatus is influenced by the integrity of the C-terminal domain of RHD3, a non-essential GTPase.