Table 3.

Proteins implicated in ppV budding

Proteins	Organism	Role in ppV budding	References
Pex29 and Pex30	S. cerevisiae	ER resident proteins that physically interact with reticulon proteins (Rtn1 and Yop1); induce membrane curvature and facilitates formation of tubular structures	122
Pex30 and Pex31	S. cerevisiae	Reticulon‐like ER‐shaping proteins predominantly localized at the pER	124
ESCRT‐III proteins (Vps20 and Snf7)	S. cerevisiae	Involved in release of ppVs from ER via membrane scissioning	121
Sec238 and Srp54	Y. lipolytica	Implicated in the exit of Pex2 and Pex16 from ER	101
Sec16B	HeLa cells	Regulates the transport of peroxisome biogenesis factors from the ER	125 126
Pex19	S. cerevisiae P. pastoris	Mediates ppV budding from ER and in intra‐ER sorting of RING peroxins	115 120
Sec20, Sec39, and Dsl1	S. cerevisiae	Secretory proteins facilitate the exit of Pex3 from the ER	127
Seipin complex	S. cerevisiae	Facilitates ppV and LD budding	128 129