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For membrane proteins, a third mechanism, based on the interaction of their transmembrane domain (TMD) with lipid microdomains, must also be considered. In this Commentary, I review evidence in favor of the idea that partitioning of TMDs into bilayer domains that are endowed with distinct physico-chemical properties plays a pivotal role in the transport of membrane proteins within the early secretory pathway. The combination of such self-organizational phenomena with canonical intermolecular interactions is most likely to control the release of membrane proteins from the ER into the secretory pathway.<\/jats:p>","DOI":"10.1242\/jcs.183335","type":"journal-article","created":{"date-parts":[[2016,3,31]],"date-time":"2016-03-31T01:38:52Z","timestamp":1459388332000},"page":"1537-1545","source":"Crossref","is-referenced-by-count":59,"title":["Getting membrane proteins on and off the shuttle bus between the endoplasmic reticulum and the Golgi complex"],"prefix":"10.1242","volume":"129","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-7537-3974","authenticated-orcid":false,"given":"Nica","family":"Borgese","sequence":"first","affiliation":[{"name":"CNR Institute of Neuroscience , Milan 20129 , Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"237","reference":[{"key":"2024061316093095000_JCS183335C1","doi-asserted-by":"publisher","first-page":"5384","DOI":"10.1073\/pnas.0710389105","article-title":"Palmitoylation and ubiquitination regulate exit of the Wnt signaling protein LRP6 from the endoplasmic reticulum","volume":"105","author":"Abrami","year":"2008","journal-title":"Proc. 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