Abstract
The Golgi apparatus is a central hub for cellular protein trafficking and signaling. Golgi structure and function is tightly coupled and undergoes dynamic changes in health and disease. A crucial requirement for maintaining Golgi homeostasis is the ability of the Golgi to target aberrant, misfolded, or otherwise unwanted proteins to degradation. Recent studies have revealed that the Golgi apparatus may degrade such proteins through autophagy, retrograde trafficking to the ER for ER-associated degradation (ERAD), and locally, through Golgi apparatus-related degradation (GARD). Here, we review recent discoveries in these mechanisms, highlighting the role of the Golgi in maintaining cellular homeostasis.
Highlights
The Golgi, first described in 1898 by Camillo Golgi, is a stacked membranous organelle that serves as a hub of protein trafficking and post-translational modifications [1,2]
Why are several mechanisms of proteasomedependent degradation at the Golgi, involving either retrieval to the endoplasmic reticulum (ER) or localized degradation, required? Second, are there specific protein determinants involved in directing substrates to these different paths? Further, what are the sensing mechanisms involved in protein-fate decisions downstream of the ER? An example suggesting that specific protein determinants may direct the route of degradation was given by the substitution of the type
Briant et al identified that aberrations in different regions in the transmembrane domain (TMD) led to distinct degradation mechanisms
Summary
The Golgi, first described in 1898 by Camillo Golgi, is a stacked membranous organelle that serves as a hub of protein trafficking and post-translational modifications [1,2]. Cellular proteasomes are considered the main degradation machinery for cytosolic proteins, while transmembrane or secreted proteins are thought to be targeted to lysosomal degradation This distinction is more complex when considering proteins along the secretory pathway, wherein proteasomes facilitate a large part of ER-associated degradation (ERAD). While it is clear that the mere distinction of cytosolic vs membranal or luminal proteins is not sufficient to explain degradation in the secretory pathway, it is intriguing to decipher the determinants that dictate selectivity and specificity of substrate degradation. Is it protein dependent or context specific?
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
