Zentrum für Molekularbiologie der Pflanzen (ZMBP)

Research Group Jürgens

Membrane traffic in development and cytokinesis
 

Research Interests

Eukaryotic cells display functionally distinct (endo)membrane compartments such as endoplasmic reticulum (ER), Golgi stacks and trans-Golgi network (TGN), endosomes and plasma membrane that exchange proteins by membrane traffic involving transport vesicles (Fig. 1). In addition to maintaining the functional organisation of the endomembrane system, membrane traffic regulates the concentration of proteins involved in development and physiology. For example, signaling peptides, receptor kinases and nutrient transporters are delivered to their sites of action along the secretory pathway from the ER, removed by endocytosis from the plasma membrane and recycled or targeted to the vacuole for degradation. This trafficking activity takes care of approximately one-third of all proteins made in plants, animals or fungi. Our research addresses mechanisms of vesicle formation and vesicle fusion in specific biological contexts.

Figure 1:  Membrane trafficking pathways in plant cells (schematic)

A secretory protein enters the endomembrane system at the ER and is transported to the Golgi using COP-II coated vesicles. At the ER exit site (ERES), SAR1 GTPase is activated by exchange factor SEC12 followed by recruitment of the COP-II coat complex. The retrieval of ER-resident proteins from the Golgi is achieved by retrograde Golgi-ER trafficking involving COP-I coated vesicles. The COP-I coat is recruited at the Golgi by ARF1 after its activation by ARF-GEFs, GNOM and GNL1. Transport of cargo proteins from cis-Golgi to trans-Golgi and from trans-Golgi to the TGN occurs via maturation. Transport from the TGN to the PM and to the cell plate is mediated by adaptin protein-1 (AP-1) complex/clathrin-coated vesicles (CCV) which are recruited by the activity of ARF-GEF BIG1-4 and ARF1. During endocytosis, vesicles are formed at the PM either by AP-2 or by TPLATE complex (TPC). The ARF-GEF BIG5 together with ARF1 regulates the endocytosis. The endocytosed proteins such as auxin-efflux transporter PIN1 are recycled back to the PM via the GNOM-positive putative recycling endosome (RE) in an ARF1-dependent manner or transported to the vacuole for degradation. The major vacuolar transport from the TGN involves maturation of the MVB from a sub-domain of the TGN followed by its fusion with the vacuole. In addition, other pathways mediated by AP-1, AP-3 and AP-4 also contribute to the post-Golgi-vacuole transport (modified from Singh and Jürgens, 2018)