1iu1: Difference between revisions

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==Overview==

The adaptor proteins AP-1 and GGA regulate membrane traffic between the, trans-Golgi network (TGN) and endosomes/lysosomes through ARF-regulated, membrane association, recognition of sorting signals, and recruitment of, clathrin and accessory proteins. The gamma 1-adaptin subunits of AP-1 and, GGA possess homologous ear domains involved in the recruitment of, accessory proteins, gamma-synergin and Rabaptin-5. The crystal structure, of the human gamma 1-adaptin ear domain consists solely of an, immunoglobulin-like fold, unlike the alpha-adaptin ear domain., Structure-based mutational analyses reveal a binding site for the, accessory proteins that is composed of conserved basic residues, indicating that the recruitment mechanism in gamma 1-adaptin and GGA is, distinct from that in alpha-adaptin.

The adaptor proteins AP-1 and GGA regulate membrane traffic between the trans-Golgi network (TGN) and endosomes/lysosomes through ARF-regulated membrane association, recognition of sorting signals, and recruitment of clathrin and accessory proteins. The gamma 1-adaptin subunits of AP-1 and GGA possess homologous ear domains involved in the recruitment of accessory proteins, gamma-synergin and Rabaptin-5. The crystal structure of the human gamma 1-adaptin ear domain consists solely of an immunoglobulin-like fold, unlike the alpha-adaptin ear domain. Structure-based mutational analyses reveal a binding site for the accessory proteins that is composed of conserved basic residues, indicating that the recruitment mechanism in gamma 1-adaptin and GGA is distinct from that in alpha-adaptin.

==About this Structure==

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[[Category: coated pits]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:15:36 2008''

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@@ Line 4: / Line 4: @@
 ==Overview==
-The adaptor proteins AP-1 and GGA regulate membrane traffic between the, trans-Golgi network (TGN) and endosomes/lysosomes through ARF-regulated, membrane association, recognition of sorting signals, and recruitment of, clathrin and accessory proteins. The gamma 1-adaptin subunits of AP-1 and, GGA possess homologous ear domains involved in the recruitment of, accessory proteins, gamma-synergin and Rabaptin-5. The crystal structure, of the human gamma 1-adaptin ear domain consists solely of an, immunoglobulin-like fold, unlike the alpha-adaptin ear domain., Structure-based mutational analyses reveal a binding site for the, accessory proteins that is composed of conserved basic residues, indicating that the recruitment mechanism in gamma 1-adaptin and GGA is, distinct from that in alpha-adaptin.
+The adaptor proteins AP-1 and GGA regulate membrane traffic between the trans-Golgi network (TGN) and endosomes/lysosomes through ARF-regulated membrane association, recognition of sorting signals, and recruitment of clathrin and accessory proteins. The gamma 1-adaptin subunits of AP-1 and GGA possess homologous ear domains involved in the recruitment of accessory proteins, gamma-synergin and Rabaptin-5. The crystal structure of the human gamma 1-adaptin ear domain consists solely of an immunoglobulin-like fold, unlike the alpha-adaptin ear domain. Structure-based mutational analyses reveal a binding site for the accessory proteins that is composed of conserved basic residues, indicating that the recruitment mechanism in gamma 1-adaptin and GGA is distinct from that in alpha-adaptin.
 ==About this Structure==
@@ Line 26: / Line 26: @@
 [[Category: coated pits]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:03:55 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:15:36 2008''