Adaptin: Difference between revisions

Latest revision as of 08:28, 28 April 2020

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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)

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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

↑ ^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
↑ 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:https://dx.doi.org/10.1128/MCB.01394-12
↑ 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:https://dx.doi.org/10.1016/j.devcel.2004.08.009
↑ 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:https://dx.doi.org/10.1083/jcb.137.4.835
↑ 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:https://dx.doi.org/10.1006/bbrc.2001.5081

References

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky

[Ad-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:https://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:https://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:https://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:https://dx.doi.org/10.1006/bbrc.2001.5081

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@@ Line 1: / Line 1: @@
-== Your Heading Here (maybe something like 'Structure') ==
+<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='1dq8' size='350' side='right' caption='Structure of HMG-CoA reductase (PDB entry [[1dq8]])' scene=''>
+'''Adaptin''' (AP) are proteins which mediate the formation of vescicles by clathrin-coated pits.<br />
-Adaptin (AP) are proteins which mediate the formation of vescicles by clathrin-coated pits.  The AP complex is a hetertetramer composed of 2 large AP: APalpha or APgamma and APbeta, a medium-size AP: APmu and small AP: APsigma.  AP complexes connect proteins and lipids to clathrin budding sites.  There are different AP complexes in mammals.
+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/6'>Inositole hexakisphosphate binding site</scene> ([[2vgl]]).<ref name="Ad">PMID:12086608</ref>
-APalpha
+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>.
-[[1b9x]], [[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 />
-APbeta
+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>.
-[[1e42]] - hAP appendage domain - human<br />
-[[2g30]] – hAP appendage domain + ARH peptide<br />
-[[2iv9]] – hAP appendage domain + eps15 peptide<br />
-[[2iv8]] – hAP appendage domain + B-arrestin peptide<br />
-[[3h1z]] – hAP appendage domain + PTDINSPKIgamma peptide<br />
-[[3hs9]] – hAP appendage domain + intersectin peptide<br />
-APgamma
+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>.
-[[1iu1]], [[2e9g]], [[4bcx]] – hAP ear domain<br />
-[[2ymt]] – hAP ear domain + peptide<br />
-[[3zhf]] – hAP ear domain + large envelope protein peptide<br />
-[[1gyu]], [[2a7b]] – mAP appendage domain <br />
-[[1gyv]], [[1gyw]], [[3zy7]] – mAP appendage domain (mutant)<br />
-APdelta
+==3D structures of adaptin==
-[[4afi]] – hAP/vesicle-associated membrane protein 7<br />
+[[Adaptin 3D structures]]
-APmu
+</StructureSection>
-[[1bw8]], [[1i31]] – rAP + EGFR peptide<br />
-[[1bxx]] – rAP + TGN38 peptide<br />
-[[1hes]] – rAP + selectin peptide<br />
-[[2bp5]] – rAP + purinoceptor peptide<br />
-[[2pr9]] – rAP + GABA receptor peptide<br />
-[[3h85]] – rAP appendage domain + PTDINSPKIgamma peptide<br />
-[[4emz]], [[4en2]] – mAP sorting motif recognition domain + nef + MHC-I<br />
-[[2vgl]] – rAPalpha + APbeta + APmu + APsigma <br />
- [[2jkr]], [[2jkt]] – mAPalpha + APbeta + APmu + APsigma + CD4 peptide<br />
-[[2xa7]] – rAPalpha + APbeta + APmu + APsigma + cargo peptide<br />
-[[1w63]] – mAPgamma + APbeta + APmu + APsigma <br />
+== References ==
-[[4hmy]] – mAPgamma + APbeta + APmu + APsigma + ADP-ribosylation factor<br />
+<references/>
+[[Category:Topic Page]]

Adaptin: Difference between revisions

Latest revision as of 08:28, 28 April 2020

3D structures of adaptin

References

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