What is the main consequence of improper protein glycosylation?

Improper protein glycosylation primarily leads to misfolding and functional deficiencies of proteins. Glycosylation is a crucial post-translational modification that involves the addition of carbohydrate moieties to proteins. This modification is essential for proper protein folding, stability, and function.

When glycosylation is incorrect, proteins may not fold into their correct three-dimensional structures, which can result in a loss of function or the production of non-functional proteins. These misfolded proteins often cannot perform their intended roles within the cell, which can lead to various cellular dysfunctions. Additionally, improperly glycosylated proteins are more likely to be recognized and targeted for degradation by cellular quality control mechanisms, further exacerbating deficiencies in protein function.

The other options relate to desirable outcomes associated with healthy protein function. Enhanced cellular communication, improved protein stability, and increased energy production are all supported by proper glycosylation. However, when glycosylation goes awry, the consequence is predominantly detrimental to the protein's structure and functioning.