Wetting and capillary condensation are thermodynamic phenomena in whic
h the special affinity of interfaces to a thermodynamic phase, relativ
e to the stable bulk phase, leads to the stabilization of a wetting ph
ase at the interfaces. Wetting and capillary condensation are here pro
posed as mechanisms that in membranes may serve to induce special lipi
d phases in between integral membrane proteins leading to long-range l
ipid-mediated joining forces acting between the proteins and hence pro
viding a means of protein organization. The consequences of wetting in
terms of protein aggregation and protein clustering are derived both
within a simple phenomenological theory as well as within a concrete c
alculation on a microscopic model of lipid-protein interactions that a
ccounts for the lipid bilayer phase equilibria and direct lipid-protei
n interactions governed by hydrophobic matching between the lipid bila
yer hydrophobic thickness and the length of the hydrophobic membrane d
omain. The theoretical results are expected to be relevant for optimiz
ing the experimental conditions required for forming protein aggregate
s and regular protein arrays in membranes.