Protein sorting depends on presence of N-terminal signal sequence or internal transmembrane domain. Secretory proteins like insulin, lysosomal cathepsins, plasma membrane receptors and Golgi glycosyltransferases harbor hydrophobic signals recognized by signal recognition particle leading to Sec61 engagement and translocation into ER lumen or membrane, then onward transport, removed from cytosol. Absence of signal leaves nascent chain completing synthesis on free ribosomes in cytoplasm where folding by Hsp70 and TRiC chaperonin occurs. Cytoskeletal proteins actin forty three kDa forming seven n
Ref:
Blobel Nobel Lecture; signal sequence free vs membrane-bound polysomes actin spectrin cytosolic.