TABLE 1.

Summary of information on VDAC3 channel activity.

Protein	mVDAC3 (Xu et al., 1999)	hVDAC3 (Checchetto et al., 2014)	hVDAC3 (Okazaki et al., 2015)	hVDAC3 (Queralt-Martín et al., 2020)	hVDAC3 (Conti Nibali et al., 2021)
Refolding detergent	5% DMSO, 2.5% Triton X-100	1% (v/v) LDAO	0,4% (v/v) LDAO	0,1% (v/v) LDAO	1% (v/v) LDAO
Reducing agent	The presence of DTT resulted in a modest increase in insertion of VDAC3 channels.	None	None	DTT	Without and with 5 mM DTT
Bilayer composition	Asolectin:cholesterol (5:1)	Asolectin (2 mg/ml)	POPE:POPC (8:2)	DOPC:DOPE:DOPG (1:1:2)	1% DiPhPC
Conductance	It does not show a clear preferred state for this channel in a phospholipid membrane.	∼90 pS in 1M KCl	∼500 pS in 250 mM KCl	∼3.9 nS in 1M KCl	In the absence of DTT ∼0.7 nS; in the presence of DTT ∼3 nS in 1M KCl
Voltage dependence	No	No	No	Yes	No A perfect overlap of the voltage dependence between all three isoforms was obtained only when the cysteines were removed from the hVDAC3 sequence
Ion selectivity	Similar to mVDAC1 and mVDAC2, mVDAC3 resulted in the same molecular weight cutoff, indicating that this protein could also form channels that allow the flux of large nonelectrolytes across the mem- brane.	N.D.	N.D.	Similar to hVDAC1	In the presence of DTT similar to hVDAC1 and hVDAC2 The results of these experiments further corroborate the importance of cysteine redox state in pore function, and they foster the hypothesis that the selectivity of the channel is correlated to the size of the unitary conductance.