Clathrin assembly protein AP-3

Murphy, Jo Ellen; Pleasure, Irene T.; Puszkin, Saul; Prasad, Kondury; Keen, James H.

doi:10.1016/s0021-9258(20)64336-8

Cited by 67 publications

(9 citation statements)

References 33 publications

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“…Summary of the structure-function studies ofAP-3. A clathrin triskelia binding site had been found in the 33-kDa N-terminal region (1,3). A high affinity inositol polyphosphate binding site had also been found in the 33-kDa N-terminal region (33).…”

Section: Discussionmentioning

confidence: 98%

“…FI-20 and AP-3 were then shown to be identical (2,27). AP-3 is a neuronalspecific (2,26,29) phosphoprotein (23,28,31,32) and glycoprotein (32), which is unusually acidic (16, 23,28), and migrates anomalously on SDS-PAGE 1 (1,16,17,23). Two primary functional activities have been found for AP-3.…”

mentioning

confidence: 97%

“…AP-3 was independently discovered in a number oflaboratories, and has been known as pp155 (28), AP180 (16), NP185 (29), and FI-20 (23,30). pp155, AP180, and NP185 were shown to be the same protein, and renamed AP-3 (1). FI-20 and AP-3 were then shown to be identical (2,27).…”

mentioning

confidence: 99%

“…AP-3 is a clathrin assembly protein (16), as well as a high affinity receptor for specific inositol polyphosphates (33). These two functions are 1 The abbreviations used are: PAGE, polyacrylamide gel electrophoresis; GST, glutathione S-transferase; BSA, bovine serum albumin; GST-AP-3, GST fused with full-length AP-3 (isoform ASI5-ASI08+); GST-C58 kDa, GST, fused with amino acids 305-744 of AP-3 (isoform ASI5-ASI08+); GST-N33 kDa, GST, fused with amino acids 1-304 of AP-3 (isoform ASI5-ASI08+); GST-CI6 kDa, GST, fused with amino acids 745-901 of AP-3 (isoform ASI5-ASI08+); GST-M42 kDa, GST, fused with amino acids 305-744 of AP-3 (isoform ASI5-ASI08+); PMSF, phenyrnethylsulfonyl fluoride; MES, 4-morpholineethanesulfonic acid.…”

mentioning

confidence: 99%

“…In order to begin to understand the structure-function relationships of AP-3, clathrin binding properties of proteolytic fragments of AP-3 were studied (1,2). It was found that the 33-kDa N-terminal region could bind to clathrin triskelia, leading to the conclusion that the 33-kDa N-terminal region was a clathrin binding domain (1). In this same study it was found that the 33-kDa N-terminal region was insufficient for clathrin assembly.…”

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Clathrin Binding and Assembly Activities of Expressed Domains of the Synapse-specific Clathrin Assembly Protein AP-3

Lafer

1995

Journal of Biological Chemistry

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We separately expressed the 58-kDa C-terminal, 42-kDa middle, 16-kDa C-terminal, and 33-kDa N-terminal regions of AP-3 (also called F1-20, AP180, NP185, and pp155), and determined their clathrin binding and assembly properties. The 58-kDa C-terminal region of AP-3 is able to bind to clathrin triskelia and assemble them into a homogeneous population of clathrin cages and will also bind to preassembled clathrin cages. The 42-kDa central region of AP-3 can bind to both clathrin triskelia and to clathrin cages, but cannot assemble clathrin triskelia into clathrin cages. The 16-kDa C-terminal region of AP-3 can bind to clathrin cages, but cannot bind to clathrin triskelia or assemble clathrin triskelia into clathrin cages. The clathrin binding activities of the 42-kDa central region and 16-kDa C-terminal region are weaker than the corresponding activity of either the 58-kDa C-terminal region or full-length AP-3. Previous efforts had mapped a clathrin binding site within the N-terminal 33 kDa of AP-3 (Murphy, J. E., Pleasure, I. T., Puszkin, S., Prasad, K., and Keen, J. H. (1991) J. Biol. Chem. 266, 4401-4408; Morris, S. A., Schroder, S., Plessmann, U., Weber, K., and Ungewickell, E. (1993) EMBO J. 12, 667-675). However, although the N-terminal 33 kDa of AP-3 is able to bind to clathrin triskelia (Murphy, J. E., Pleasure, I. T., Puszkin, S., Prasad, K., and Keen, J. H. (1991) J. Biol. Chem. 266, 4401-4408; Ye, W., and Lafer, E. M. (1995) J. Neurosci. Res. 41, 15-26), it does not promote their assembly into clathrin cages (Murphy, J. E., Pleasure, I. T., Puszkin, S., Prasad, K., and Keen, J. H. (1991) J. Biol. CHem. 266, 4401-4408; Ye, W., and Lafer, E. M. (1995) J. Neurosci. Res. 41, 15-26) or bind to preassembled clathrin cages (Ye, W., and Lafer, E. M. (1995) J. Neurosci. Res. 41, 15-26). It appears that the smallest functional unit that carries out all of the reported clathrin binding and assembly properties of AP-3, essentially as well as the full-length protein, is the 58-kDa C-terminal region.

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Section: Discussionmentioning

confidence: 98%

mentioning

confidence: 97%

mentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

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Clathrin Binding and Assembly Activities of Expressed Domains of the Synapse-specific Clathrin Assembly Protein AP-3

Lafer

1995

Journal of Biological Chemistry

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A novel AP180-related protein in vesicles that concentrate at acetylcholine receptor clusters

et al. 1998

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Monoclonal antibodies were generated to vesicular membranes of clathrin coated vesicles enriched for acetylcholinesterase (AChE). One of these, C172, recognizes vesicles which accumulate in muscle cells around nuclei associated with acetylcholine receptor AChR clusters. Immunoblots of muscle extracts and brain purified clathrin coated vesicles show that C172 recognizes a 100 kd band in muscle, but a 180 kd band in brain. Western blots of purified AP180 protein stained with the two antibodies AP180.1 and C172 displayed the same staining pattern. Tryptic digests probed with peptide antibodies (PS26 and PS27) generated to known sequences of AP180 were used to map the epitope for C172 within the brain AP180 sequence. On immunoblots of digested AP180, all AP180 antibodies and C172 recognized a 100 kd tryptic fragment, however only C172 recognized a smaller 60 kd. Our results suggest that the C172 epitope is located within amino acids 305-598 of the AP180 sequence. Confocal fluorescence microscopy of myoblasts and myotubes stained with the C172 antibody gives a punctate immunofluorescence pattern. Myoblasts stained with C172 revealed a polarized distribution of vesicles distinct from that observed when cells are stained with gamma adaptin antibody which is known to localize to trans Golgi network. Myotubes stained with C172 antibody reveal a linear array of vesicular staining. Quantitative analysis of C172 reactive vesicles revealed a significant increase in number of vesicles present around the nuclei associated with the acetylcholine receptor clusters. These vesicles did not colocalize with the Golgi cisternae. These results indicate that a protein with homology to the neuron-specific coated vesicle protein AP180, is present in muscle cells associated with vesicles showing significant concentration around postsynaptic nuclei present in close proximity to AChR clusters.

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The mechanism of receptor‐mediated endocytosis: More questions than answers

Schmid

1992

BioEssays

100

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Receptor-mediated endocytosis occurs via clathrin-coated pits and is therefore coupled to the dynamic cycle of assembly and disassembly of the coat constituents. These coat proteins comprise part, but certainly not all, of the machinery involved in the recognition of membrane receptors and their selective packaging into transport vesicles for internalization. Despite considerable knowledge about the biochemistry of coated vesicles and purified coat proteins, little is known about the mechanisms of coated pit assembly, receptor-sorting and coated vesicle formation. Cell-free assays which faithfully reconstitute these events provide powerful new tools with which to elucidate the overall mechanism of receptor-mediated endocytosis.

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Clathrin assembly protein AP-3

Cited by 67 publications

References 33 publications

Clathrin Binding and Assembly Activities of Expressed Domains of the Synapse-specific Clathrin Assembly Protein AP-3

Clathrin Binding and Assembly Activities of Expressed Domains of the Synapse-specific Clathrin Assembly Protein AP-3

A novel AP180-related protein in vesicles that concentrate at acetylcholine receptor clusters

The mechanism of receptor‐mediated endocytosis: More questions than answers

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