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Table 2 Proteins triggering membrane proliferation in eukaryotes

From: Inducible intracellular membranes: molecular aspects and emerging applications

Protein Organism
Origin Expressed Morphology Target organelle Observations Refs.
HMG-CoA S. cerevisiae
S. pombe
S. cerevisiae karmellae” stacked membranes around nucleus ER Soluble domain not required.
Transmembrane helix alone not sufficient.
[98, 135, 150]
Cytochrome b5 R. norvegicus S. cerevisiae karmellae” stacked membranes around nucleus ER Transmembrane domain disturbed by proline hinders membrane proliferation [132]
Cytochrome P450 C. maltosa S. cerevisiae karmellae” stacked membranes around nucleus + Tubules ER Minimum domain 1–33: contains hydrophobic helix and charged residues flanking it. [129, 134, 220,221,222]
PMA2 (H+ ATPase) S. cerevisiae S. cerevisiae Tubules ER [223]
RRp − 180 kDa C. lupus S. cerevisiae karmellae” stacked membranes around nucleus ER RBS not required for membrane proliferation.
Increase of secretory pathway
[130, 224]
D2S receptor H. sapiens P. pastoris karmellae” stacked membranes around nucleus ER [225]
sk2 Channel H. sapiens P. pastoris karmellae” stacked membranes around nucleus and ER ER [226]
B2 receptor H. sapiens P. pastoris karmellae” stacked membranes around nucleus ER [227]
LaminB receptor G. domesticus S. cerevisiae karmellae” stacked membranes around nucleus ER [228]
Pex12p S. cerevisiae S. cerevisiae Multilayered membranes Peroxisome Observed morphology is dependent on expression level [131]
Pex15p S. cerevisiae S. cerevisiae Multilayered membranes Peroxisome, ER ER to peroxisome transport blocked [210]
2BC Poliovirus S. cerevisiae Vesicles Vacuole ER transport blocked [99]
36 k protein IRV Carnation Italian Ringspot Virus S. cerevisiae Vesicles Mitochondria [133]
Protein A Flock House Virus S. cerevisiae Vesicles Mitochondria Retargeting of protein A to ER possible with ER specific sequence [151]
  1. All listed proteins are transmembrane proteins