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. Author manuscript; available in PMC: 2010 Oct 1.
Published in final edited form as: Int J Biochem Cell Biol. 2009 Apr 21;41(10):1817–1827. doi: 10.1016/j.biocel.2009.04.010

Table 1.

Summary of cited proteins involved in ER-Mitochondria structural link

SYMBOL FULL NAME DETAILS
ER and Mitochondria structure
CaBPs Ca2+-binding proteins Large family of eukaryotic proteins containing a specific helix-loop-helix structure, referred to as the EF-hand motif; many of the Ca2+-mediated processes are carried out through the cooperation of CaBPs
IP3Rs Inositol-1,4,5-trisphosphate receptors Family of ligand-gated channels that function to release Ca2+ from intracellular Ca2+ stores (ER and Golgi apparatus) in response to agonist stimulation
RyRs Ryanodine receptors Ca2+ release channels located in the Sarcoplasmic Reticulum membrane
SERCA Sarco-Endoplasmic Reticulum Ca2+- ATPase Highly conserved family of Ca2+ pumps which actively transfer Ca2+ from the cytosol to the lumen ER/SR at the expense of ATP hydrolysis
VDAC Voltage dependent anion channel The VDAC family of proteins are the most abundant proteins of the outer mitochondrial membrane and mediate the flow of ions and metabolites between the cytosol and the mitochondrial intermembrane space
ER and Mitochondria dynamics
DRP1 Dynamin-related protein 1 Main protein controlling mitochondrial fission in mammalian cells. DRP-1 is located in the cytoplasm but during fission translocates to mitochondria surface, where constriction of the membranes takes place by direct or indirect interaction with hFis1, its adaptor in the OMM
Mfn1 and Mfn2 Mitofusins 1 and 2 GTPases localized to the outer mitochondrial membrane, playing a pivotal role in mitochondrial fusion
OPA1 Optic Atrophy 1 Profusion dynamin-related protein of the inner mitochondrial membrane mutated in dominant optic atrophy; this protein has been recently shown to participate in the biogenesis of the mitochondrial cristae and regulate the cristae remodelling pathway
PARL Presenilin-associated rhomboid like Rhomboid protease of the inner mitochondrial membrane (originally identified in a yeast two-hybrid screen as an interactor of presenilin) required for the correct assembly of the OPA1-containing structures that regulate the integrity of the mitochondrial cristae junctions