Some extracellular ligands that bind to specific cell-surface receptors are internalized, along with their receptors, in clathrin-coated vesicles. This endocytic pathway delivers some ligands (e.g., LDL particles) to lysosomes, where they are degraded. Transport vesicles from the cell surface first fuse with late endosomes, which subsequently fuse with lysosomes. Most receptor-ligand complexes dissociate in the acidic milieu of the late endosome; the receptors are recycled to the plasma membrane, while the ligands are sorted to lysosomes.

recent report demonstrate that aggregate form of some protein can bind to integrain (doi: 10.1074/jbc.M115.678177) and variety of receptor on plasma membrane (doi: 10.2174/1389203043486937).

internalization of abnormal protein to other cell have been demonestrated. for example in liver, abnormal glycoproteins (asialoglycoprotein) whose oligosaccharides terminate in galactose rather than the normal sialic acid, bind and internalize through liver-specific receptor mediates pathway. Electron microscopy of liver cells perfused with asialoglycoprotein reveal that 5–10 minutes after internalization, asialoglycoprotein are found in the lumen of late endosomes, while the tubular membrane extensions are rich in receptor and rarely contain asialoglycoprotein. 

Dear Behnam, Thank you for  very useful and interesting discussion. As you have written, this kind of endocytic pathway may be  for recycle active receptors on the plasma membrane. However, the aggregated forms of different peptides and proteins have different structures and characters. It means that receptors can interact non specifically  to the different aggregated particles.  

I hope my recent paper regarding the transmission phenomenon of aSYN would be helpful for you.

https://www.ncbi.nlm.nih.gov/pubmed/28539529