The ∼ 16 kDa C-terminal sequence of clathrin assembly protein AP180 is essential for efficient clathrin binding.

Abstract

Brain-specific AP180 is present in clathrin coats at equal concentration to the adapter complex, AP2, and assembles clathrin faster than any other protein in vitro. Both AP180 and its ubiquitously expressed homolog clathrin assembly lymphoid myeloid leukemia protein (CALM) control vesicle size and shape in clathrin mediated endocytosis. The clathrin assembly role of AP180 is mediated by a long disordered C-terminal assembly domain. Within this assembly domain, a central acidic clathrin and adapter binding (CLAP) sub-domain contains all of the known short binding motifs for clathrin and AP2. The role of the remaining ∼ 16 kDa C-terminal sequence has not been clear. We show that this sequence has a separate function in ensuring efficient binding of clathrin, based on in vitro binding and ex vivo transferrin uptake assays. Sequence alignment suggests the C-terminal sub-domain is conserved in CALM.

• Authors: Ling-Shan Chan, Lia Moshkanbaryans, Jing Xue, Mark E Graham
• Journal: PloS one (PLoS One) Vol. 9 Issue 10 Pg. e110557 ( 2014) ISSN: 1932-6203 [Electronic] United States
• PMID: 25329427 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Clathrin
• Monomeric Clathrin Assembly Proteins
• PICALM protein, mouse
• clathrin assembly protein AP180

Topics

• Amino Acid Motifs
• Amino Acid Sequence
• Animals
• COS Cells
• Chlorocebus aethiops
• Clathrin (chemistry, genetics, metabolism)
• Mice
• Monomeric Clathrin Assembly Proteins (chemistry, genetics, metabolism)
• Protein Binding
• Protein Structure, Tertiary