Structuring of the endolysosomal system by HOPS and CORVET tethering complexes

Eukaryotic cells depend on their endolysosomal system for membrane protein and organelle turnover, plasma membrane quality control, or regulation of their nutrient uptake. All material eventually ends up in the lytic environment of the lysosome for cellular recycling. At endosomes and lysosomes, the multisubunit complexes CORVET and HOPS tether membranes by binding both their cognate Rab GTPase and specific membrane lipids. Additionally, they carry one Sec1/Munc18-like subunit at their center and thus promote SNARE assembly and, subsequently, bilayer mixing. Recent structural and functional analysis provided insights into their organization and suggested how these complexes combine tethering with fusion catalysis. This review discusses the function and structural organization of HOPS and CORVET in the context of recent studies in yeast and metazoan cells.