Related Experiment Videos
ER-mitochondria contact sites in yeast: beyond the myths of ERMES
Alexander Lang1, Arun T John Peter1, Benoît Kornmann1
1Institute of Biochemistry, ETH Zurich, 8093 Zürich, Switzerland.
Abstract:
A standout feature of eukaryotic cells is the presence of organelles with distinct chemical compositions and physical properties, which aid in the accomplishment of specialized metabolic tasks. This complex topology, however, makes a permanent crosstalk between the organelles a necessity for the coordination of cellular function. While molecule exchange between organelles via the vesicular transport system has been extensively studied, communication via direct connections has only recently become a new matter of interest. These direct connections termed membrane contact sites (MCSs) represent zones of close proximity (10-30nm) between two organelles. Research in the past years has revealed a number of MCSs especially between the ER and almost every other organelle [1(•)]. In particular, the MCSs between the ER and the mitochondria have undergone intense investigation. While the quest for ER-mitochondria MCS components in human cells has led to the revelation of an ever growing number of potential factors, studies in the simpler eukaryote Saccharomyces cerevisiae revealed the actual existence of a molecular tether between the two organelles [2(••)].
Related Concept Videos
The Inner Mitochondrial Membrane
Translocation of Proteins into the Mitochondria
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
Yeast Signaling
Mitochondrial Membranes
Mitochondrial Membranes
Porin Insertion in the Outer Mitochondrial Membrane
Three models describe the assembly of porins by the SAM complex and their insertion into the outer membrane. Model 1 suggests that porins are assembled outside the SAM channel as the...