You can choose from almost all of the columns that are used for other proteins, but remember that your crude sample and partially purified fractions will contain a detergent. Hence, hydrophobic interaction chromatography and reverse phase are probably not something you should consider. If you have an uncharged detergent (e.g. triton, tween20) you can used ion exchange and most other chromatography modes without worrying about detergent interactions. For gel filtration, the protein will be protected by a micelle of detergent, increasing its size and that of other membranes proteins in the mixture, and the resolution is often not great as a result. In addition to chromatography, if you can use Triton x114 for solubilization, you can exploit phase separation as a separation step.
Does it carry a fusion or epitope tag?... If yes, affinity resins would be the first choice indeed. You can perform IEX, SEC, or CHT as clean-up. Otherwise, I suggest using multi-mode chromatography resins as capturing mode of purification...Other than, FPLC, I recommend pull-down assays and if the activity is not necessary, gel electrophoresis is also a good option to purify the membrane protein.
I would personally recommend an affinity chromatography using a C-terminally fused Rho1D4-tag. Potentially followed by a Size-Exclusion chromatography.
Membrane proteins always have a low abundance you it is best to settle for high-purity, lower yield purification techniques.