Heilker R, Spiess M, Crottet P
University of Basel, Switzerland.
Bioessays. 1999 Jul;21(7):558-67. doi: 10.1002/(SICI)1521-1878(199907)21:7<558::AID-BIES4>3.0.CO;2-R.
Sorting of membrane proteins is generally mediated by cytosolic coats, which create a scaffold to form coated buds and vesicles and to selectively concentrate cargo by interacting with cytosolic signals. The classical paradigm is the interaction between clathrin coats and associated adaptor proteins, which cluster receptors with characteristic tyrosine and dileucine motifs during endocytosis. Clathrin in association with different sets of adaptors is found in addition at the trans-Golgi network and endosomes. Sequences similar to internalization signals also direct lysosomal and basolateral sorting, which implicates related clathrinadaptor coats in the respective sorting pathways. This review concentrates on the recognition of sorting signals by clathrin-associated adaptor proteins, an area of significant recent progress due to new methodological and conceptual approaches.
膜蛋白的分选通常由胞质包被介导，胞质包被形成一个支架以形成包被小芽和小泡，并通过与胞质信号相互作用来选择性地浓缩货物。经典模式是网格蛋白包被与相关衔接蛋白之间的相互作用，在胞吞作用期间，这些衔接蛋白将具有特征性酪氨酸和双亮氨酸基序的受体聚集在一起。此外，在反式高尔基体网络和内体中也发现了与不同衔接蛋白组合相关的网格蛋白。与内化信号相似的序列也指导溶酶体和基底外侧分选，这意味着在各自的分选途径中存在相关的网格蛋白衔接蛋白包被。本综述集中于网格蛋白相关衔接蛋白对分选信号的识别，由于新的方法和概念方法，这是一个近期取得重大进展的领域。
