The positive-inside rule dictates the distribution of charged residues in membrane proteins
Multiple studies and foundational rules confirm that the positive-inside rule dictates the asymmetric distribution of charged residues (particularly lysine and arginine) to determine the orientation and topogenesis of membrane proteins.
The retrieved literature robustly supports the claim. Papers [0], [1], [4], [7], [8], [9], [10], and [11] all explicitly discuss or utilize the positive-inside rule as a fundamental determinant of membrane protein topology and charged residue distribution across the membrane. There are no refuting papers.
M. Bogdanov, Jun Xie, W. Dowhan. Lipid-Protein Interactions Drive Membrane Protein Topogenesis in Accordance with the Positive Inside Rule*. 2009. https://doi.org/10.1074/jbc.R800081200
Positively and negatively charged amino acids in extramembrane domains act as determinants of membrane protein orientation.
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Assaf Elazar, Jonathan Jacob Weinstein, Jaime Prilusky, Sarel Jacob Fleishman. Interplay between hydrophobicity and the positive-inside rule in determining membrane-protein topology. 2016. https://doi.org/10.1073/pnas.1605888113
The positive-inside rule orients segments with respect to the membrane and drives insertion.
Haruki Hasegawa, N. Patel, E. Ettehadieh, Peng Li, A. Lim. Topogenesis and cell surface trafficking of GPR34 are facilitated by positive-inside rule that effects through a tri-basic motif in the first intracellular loop.. 2016. https://doi.org/10.1016/j.bbamcr.2016.04.010
A tri-basic motif acts as a topogenic signal dictating transmembrane domain orientation via the positive-inside rule.
G von Heijne. Membrane protein structure prediction. Hydrophobicity analysis and the positive-inside rule.. 1992. https://doi.org/10.1016/0022-2836(92)90934-c
Bacterial inner membrane protein topology prediction relies successfully on the positive-inside rule.
William Dowhan, Mikhail Bogdanov. Lipid-dependent membrane protein topogenesis.. 2009. https://doi.org/10.1146/annurev.biochem.77.060806.091251
Positively charged residues act as retention signals that determine membrane protein topology alongside lipid interactions.
William Dowhan, Heidi Vitrac, Mikhail Bogdanov. Lipid-Assisted Membrane Protein Folding and Topogenesis.. 2019. https://doi.org/10.1007/s10930-019-09826-7
The positive-inside rule governs transmembrane protein folding and topogenesis, sometimes extended to a charge balance rule.
Catherine A Charneski, Laurence D Hurst. Positive charge loading at protein termini is due to membrane protein topology, not a translational ramp.. 2014. https://doi.org/10.1093/molbev/mst169
N-terminal positive charge loading is explicitly explained by the membrane orientation rules of the positive-inside rule.
L I Krishtalik, W A Cramer. On the physical basis for the cis-positive rule describing protein orientation in biological membranes.. 1995. https://doi.org/10.1016/0014-5793(95)00756-y
The asymmetry of positively charged residues on membrane sides characterizes hydrophobic intramembrane protein topology.
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