A way to regulate function of membrane protein is to control its amount and trafficking into proper cellular compartment. Here, we report the molecular mechanism, how adhesion protein in combination with set of ubiquitin ligases can quantitatively monitor the transport of a specific membrane protein along the secretory and endocytic pathway. A leukodystrophy called MLC, results from defect in protein MLC1 or adhesion protein GlialCAM. We found that GlialCAM is indispensable during biosynthesis by protecting MLC1 against the endoplasmic reticulum associated degradation and promoting its biosynthetic maturation. Formation of MLC1/GlialCAM complex ensures the escape of native, but also the misfolded MLC1 to the plasma membrane and endosomes. Aberrant MLC1 forms are then disposed by CHIP and Ubr1 mediated ubiquitination leading to ESCRT-dependent lysosomal degradation. Thus, the interplay of the endoplasmic reticulum and plasma membrane quality control and the unusual chaperoning of GlialCAM toward MLC1 folding intermediates determines the proper functional expression level of MLC1.