Yes, there are many methods to display proteins on the cell surface. Check for papers on "surface display" http://scholar.google.ch/scholar?hl=en&q=surface+display&btnG=&as_sdt=1%2C5&as_sdtp=

, . e.g. "Yeast surface display". Cell surface display is frequently used for selection of functional proteins from gene libraries, as an alternative to ribosome display and phage display. The gene for the protein of interest is fused to an anchoring motif, e.g. the gene of a cell surface protein. Cells that produce a fusion protein with the desired functional characteristics, eg. binders for a specific target, can then be selected by Fluorescence activated cell sorting, if a fluorescence-labelled target is used.

If you want to express an intracellular protein on the cell surface, I'd suggest you add an N-terminal signaling peptide and a membrane anchor - such as a transmembrane helix or GPI-anchor to the gene of interest.

Agreed with previous answer. It would need to be an engineered protein sequence, using modular transmembrane motifs, at the least. It could be checked for localization using fluorescence techniques. It should also be possible to engineer it with release mechanisms for only the sequence of interest, such as enzyme consensus sites or even something like a disulfide linkage.

Yes, there are many methods to display proteins on the cell surface. Check for papers on "surface display" http://scholar.google.ch/scholar?hl=en&q=surface+display&btnG=&as_sdt=1%2C5&as_sdtp=

, . e.g. "Yeast surface display". Cell surface display is frequently used for selection of functional proteins from gene libraries, as an alternative to ribosome display and phage display. The gene for the protein of interest is fused to an anchoring motif, e.g. the gene of a cell surface protein. Cells that produce a fusion protein with the desired functional characteristics, eg. binders for a specific target, can then be selected by Fluorescence activated cell sorting, if a fluorescence-labelled target is used.