Adaptin: Difference between revisions

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<StructureSection load='2vgl' size='350' side='right' caption='Structure of Adaptin core: AP-α-2 (cyan), AP-β-1 (magenta), AP-μ-1 (green), AP-σ-1 (olive) complex with inositole hexakisphosphate  (PDB entry [[2vgl]])' scene='55/559108/Cv/1'>
<StructureSection load='2vgl' size='350' side='right' caption='Structure of Adaptin core: AP-α-2 (cyan), AP-β-1 (magenta), AP-μ-1 (green), AP-σ-1 (olive) complex with inositole hexakisphosphate  (PDB entry [[2vgl]])' scene='55/559108/Cv/1'>
'''Adaptin''' (AP) are proteins which mediate the formation of vescicles by clathrin-coated pits. The AP complex is a heterotetramer composed of 2 '''large AP''': AP-α or AP-γ and AP-β, a '''medium-size AP''': AP-μ and '''small AP''': AP-σ.  AP complexes connect proteins and lipids to clathrin budding sites.  There are different AP complexes in mammals.<ref name="Ad">PMID:12086608</ref>
'''Adaptin''' (AP) are proteins which mediate the formation of vescicles by clathrin-coated pits.<br />
The '''AP-2 complex''' is a heterotetramer composed a core domain containing 2 '''large AP''': AP-α or AP-γ and AP-β, a '''medium-size AP''': AP-μ and '''small AP''': AP-σ, 2 appendage domains or '''EAR'''.  The core domain binds to the membrane and to cargo proteins which should be internalized and the EAR domains bind to clathrin and accessory proteins.  There are different AP complexes in mammals.<ref name="Ad">PMID:12086608</ref>
*<scene name='55/559108/Cv/3'>Adaptin core: AP-α-2, AP-β-1, AP-μ-1, AP-σ-1 complex with inositole hexakisphosphate</scene>.
*<scene name='55/559108/Cv/3'>Adaptin core: AP-α-2, AP-β-1, AP-μ-1, AP-σ-1 complex with inositole hexakisphosphate</scene>.
*<scene name='55/559108/Cv/6'>Inositole hexakisphosphate binding site</scene> ([[2vgl]]).<ref name="Ad">PMID:12086608</ref>
*<scene name='55/559108/Cv/6'>Inositole hexakisphosphate binding site</scene> ([[2vgl]]).<ref name="Ad">PMID:12086608</ref>
The '''AP-1 complex''' heterotetramer μ subunit packages insulin receptor substrates into clathrin-coated vescicles.  This is needed for insulin/insulin-like growth factor bioactivities including mitogenesis<ref>PMID:23478262</ref>.
The '''AP-3 complex''' heterotetramer is involved in the biogenesis of lysosome-related organelles<ref>PMID:15469849</ref>.  It contains subunits β3, μ3, δ and σ3<ref>PMID:9151686</ref>.
The '''AP-4 complex''' heterotetramer is involved in the targeting proteins from the trans-Golgi network (TGN) to yhr endosomal-lysosomal system.  It contains subunits β-type, μ-type, ε and σ-type<ref>PMID:11409905</ref>.


==3D structures of adaptin==
==3D structures of adaptin==
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</StructureSection>
</StructureSection>


===3D structures of adaptin===
Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
{{#tree:id=OrganizedByTopic|openlevels=0|
*AP-α-2
**[[1b9k]], [[1qts]] – mAP appendage domain – mouse<br />
**[[1qtp]] – mAP appendage domain (mutant)<br />
**[[1ky6]], [[1kyd]] – mAP appendage domain + epsin peptide<br />
**[[1ky7]] – mAP appendage domain + amphiphysin peptide<br />
**[[1kyf]], [[1kyu]] – mAP appendage domain + eps15 peptide<br />
**[[1w80]], [[2vj0]] – mAP appendage domain + synaptojanin peptide<br />
**[[3hs8]] – mAP appendage domain + intersectin peptide<br />
*AP-β
**[[1e42]] – hAP-1 appendage domain - human<br />
**[[2g30]] – hAP-1 appendage domain + ARH peptide<br />
**[[3h1z]] – hAP-1 appendage domain + PTDINSPKI-γ peptide<br />
**[[3hs9]] – hAP-1 appendage domain + intersectin peptide<br />
**[[2iv9]] – hAP-2 appendage domain + eps15 peptide<br />
**[[2iv8]] – hAP-2 appendage domain + B-arrestin peptide<br />
**[[1mj7]] – hAP-4 appendage domain <br />
*AP-γ
**[[1iu1]] – hAP-1 ear domain<br />
**[[1gyu]], [[2a7b]] – mAP-1 appendage domain <br />
**[[1gyv]], [[1gyw]], [[3zy7]] – mAP-1 appendage domain (mutant)<br />
**[[2e9g]], [[4bcx]] – hAP-2 ear domain<br />
**[[2ymt]] – hAP-2 ear domain + peptide<br />
**[[3zhf]] – hAP-2 ear domain + large envelope protein peptide<br />
*AP-δ-1
**[[4afi]] – hAP-1/vesicle-associated membrane protein 7<br />
*AP-μ
**[[3h85]] – rAP-1 appendage domain + PTDINSPKIγ peptide<br />
**[[4emz]], [[4en2]] – mAP-1 sorting motif recognition domain + nef + MHC-I<br />
**[[2bp5]] – rAP-2 + purinoceptor peptide<br />
**[[1bw8]], [[1i31]] – rAP-2 C-terminal + EGFR peptide<br />
**[[1bxx]] – rAP-2 C-terminal + TGN38 peptide<br />
**[[1hes]] – rAP-2 C-terminal + selectin peptide<br />
**[[5c7z]], [[5fpi]] – rAP-2 C terminal + integrin peptide<br />
**[[2pr9]] – rAP-2 C-terminal + GABA receptor peptide<br />
**[[5wrm]], [[5wrl]], [[5wrk]] – rAP-2 C-terminal + insulin receptor substrate peptide <br />
**[[4ikn]] – rAP-3 + TGN38 sorting peptide <br />
**[[3l81]], [[4mdr]] – hAP-4 + amyloid beta-A4 peptide <br />
**[[6bnt]] – hAP-2 C-terminal + insulin receptor substrate peptide <br />
*AP-α2 + AP-σ
**[[4nee]] – rAP-2 + HIV-1 NEF <br />
*AP-α2 + AP-β + AP-σ
**[[4uqi]] – rAP-2 + VPU <br />
*AP-α + AP-β + AP-μ + AP-σ
**[[2vgl]] – rAPα-2 + APβ-1 + APμ-1 + APσ-1 <br />
**[[4uqi]] – rAPα-2 + APβ-2 + APμ-2 + APσ-1 <br />
**[[2jkr]], [[2jkt]] – mAPα-2 + APβ-1 + APμ-1 + APσ-1 + CD4 peptide<br />
**[[2xa7]] – rAPα-2 + APβ + APμ + APσ + cargo peptide<br />
*AP-β-1 + AP-γ-1 + AP-μ-1 + AP-σ-3
**[[6dff]], [[6d84]], [[6d83]], [[6cri]], [[6cm9]] – hAPβ-1 + APμ-1 + APσ-3 + ARF1 + tetherin-NEF – Cryo EM <br />
*AP-γ + AP-β + AP-μ + AP-σ


**[[1w63]] – mAP-1  <br />
**[[4hmy]] – mAP-1 + ADP-ribosylation factor<br />
**[[4p6z]] – mAP-1 + VPU + bone marrow stromal antigen<br />
}}
== References ==
== References ==
<references/>
<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Latest revision as of 11:28, 28 April 2020

Adaptin (AP) are proteins which mediate the formation of vescicles by clathrin-coated pits.

The AP-2 complex is a heterotetramer composed a core domain containing 2 large AP: AP-α or AP-γ and AP-β, a medium-size AP: AP-μ and small AP: AP-σ, 2 appendage domains or EAR. The core domain binds to the membrane and to cargo proteins which should be internalized and the EAR domains bind to clathrin and accessory proteins. There are different AP complexes in mammals.[1]

The AP-1 complex heterotetramer μ subunit packages insulin receptor substrates into clathrin-coated vescicles. This is needed for insulin/insulin-like growth factor bioactivities including mitogenesis[2].

The AP-3 complex heterotetramer is involved in the biogenesis of lysosome-related organelles[3]. It contains subunits β3, μ3, δ and σ3[4].

The AP-4 complex heterotetramer is involved in the targeting proteins from the trans-Golgi network (TGN) to yhr endosomal-lysosomal system. It contains subunits β-type, μ-type, ε and σ-type[5].

3D structures of adaptin

Adaptin 3D structures


Structure of Adaptin core: AP-α-2 (cyan), AP-β-1 (magenta), AP-μ-1 (green), AP-σ-1 (olive) complex with inositole hexakisphosphate (PDB entry 2vgl)

Drag the structure with the mouse to rotate


ReferencesReferences

  1. ↑ 1.0 1.1 Collins BM, McCoy AJ, Kent HM, Evans PR, Owen DJ. Molecular architecture and functional model of the endocytic AP2 complex. Cell. 2002 May 17;109(4):523-35. PMID:12086608
  2. ↑ Yoneyama Y, Matsuo M, Take K, Kabuta T, Chida K, Hakuno F, Takahashi S. The AP-1 complex regulates intracellular localization of insulin receptor substrate 1, which is required for insulin-like growth factor I-dependent cell proliferation. Mol Cell Biol. 2013 May;33(10):1991-2003. doi: 10.1128/MCB.01394-12. Epub 2013, Mar 11. PMID:23478262 doi:http://dx.doi.org/10.1128/MCB.01394-12
  3. ↑ Lefrancois S, Janvier K, Boehm M, Ooi CE, Bonifacino JS. An ear-core interaction regulates the recruitment of the AP-3 complex to membranes. Dev Cell. 2004 Oct;7(4):619-25. doi: 10.1016/j.devcel.2004.08.009. PMID:15469849 doi:http://dx.doi.org/10.1016/j.devcel.2004.08.009
  4. ↑ Simpson F, Peden AA, Christopoulou L, Robinson MS. Characterization of the adaptor-related protein complex, AP-3. J Cell Biol. 1997 May 19;137(4):835-45. doi: 10.1083/jcb.137.4.835. PMID:9151686 doi:http://dx.doi.org/10.1083/jcb.137.4.835
  5. ↑ Takatsu H, Futatsumori M, Yoshino K, Yoshida Y, Shin HW, Nakayama K. Similar subunit interactions contribute to assembly of clathrin adaptor complexes and COPI complex: analysis using yeast three-hybrid system. Biochem Biophys Res Commun. 2001 Jun 22;284(4):1083-9. doi:, 10.1006/bbrc.2001.5081. PMID:11409905 doi:http://dx.doi.org/10.1006/bbrc.2001.5081

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