Autophagy-related protein: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<scene name='70/708076/Cv/2'>Zn+2 ion is bound with 4 Cys residues</scene> in yeast Atg7 C-terminal domain.  
<scene name='70/708076/Cv/2'>Zn+2 ion is bound with 4 Cys residues</scene> in yeast Atg7 C-terminal domain.<ref>PMID:22055191</ref>
</StructureSection>
</StructureSection>



Revision as of 12:33, 13 December 2015

Autophagy-related proteins (Atg) function in autophagosome formation from the pre-autophagosomal structure (PAS). The phagosomes perform protein degradation under starvation. Autophagy is the process of forming a vacuole around proteins or nucleic acids destined to be broken down. This vacuole is a double membrane enclosure called phagophore. Atgs have non-autophagic functions as well as they are involved in cell survival and apoptosis.[1] So far 34 Atgs have been identified in yeast.

  • Atg1, 6, 14 are involved in the formation of the phagophore.
  • Atg3 catalyzes the conjugation of Atg8 and phosphatidylethanolamine. This conjugation is essential for autophagosome formation.
  • Atg4, 5, 7, 10, 16 are involved in the maturation of the phagophore.
  • Atg8 is structurally similar to ubiquitin. It is a targeting factor in cytoplasm-to-vacuole transport of proteins such as aminopeptidase and a-mannosidase. Microtubule-associated protein light chain 3 LC3 is a mammalian Atg8.
  • Atg12 is involved in the elongation of the phagophore.
  • Atg13, 17 are PAS scaffold proteins.
  • Atg101 is believed to protect Atg13 from proteasomal degradation.

Structural highlights

in yeast Atg7 C-terminal domain.[2]

Yeast Atg7 C terminal (green) complex with Atg8 (magenta) and Zn+2 ion (grey) (PDB code 3vh3)

Drag the structure with the mouse to rotate

3D Structures of autophagy-related protein3D Structures of autophagy-related protein

Updated on 13-December-2015

    • 2dyt – yAtg3 – yeast
  • Autophagy-related protein 4
  • Autophagy-related protein 5
    • 3vqi – KmAtg5 – Kluyveromyces marxianus
    • 4tq1 – hAtg5 + TECAIR peptide
  • Autophagy-related protein 7
  • Autophagy-related protein 8
    • 2kq7 – yAtg8 - NMR
    • 2kwc – yAtg8 (mutant) - NMR
    • 3m95 – Atg8 – silk worm
  • Autophagy-related protein 10
  • Autophagy-related protein 12
    • 1wz3 – AtAtg12B – Arabidopsis thaliana
  • Autophagy-related protein 16
    • 3a7o – yAtg16 coiled-coil domain
    • 3a7p – yAtg16 coiled-coil domain (mutant)
  • Autophagy-related protein 19
    • 2kzb – yAtg19 a-mannosidase binding domain - NMR
  • Autophagy-related protein 101
  • Autophagy-related protein 1+13
    • 4p1n – KmAtg1 + KmAtg13
  • Autophagy-related protein 3+5+12+16
    • 4naw – hAtg3 peptide + hAtg5 + hAtg12 + hAtg16-1 N terminal
  • Autophagy-related protein 5+12+16
    • 4gdk, 4gdl – hAtg5 + hAtg12 + hAtg16-1 N terminal
    • 3w1s – yAtg5 + yAtg12 + yAtg16 N terminal
  • Autophagy-related protein 5+16
    • 2dym, 2dyo – yAtg5 + yAtg16 N terminal
    • 4tq0 – hAtg5 + hAtg16-1 N terminal
  • Autophagy-related protein 7+3
    • 3t7g – yAtg7 N terminal + yAtg3 peptide
    • 4gsl – yAtg7 + yAtg3 (mutant)
    • 3vx8 – AtAtg7 N terminal + AtAtg3
  • Autophagy-related protein 7+8
    • 3vh3 – yAtg7 C terminal + yAtg8 (mutant)
    • 2li5 – yAtg7 peptide + yAtg8 (mutant)
    • 3rui – yAtg7 C terminal (mutant) + yAtg8
    • 3vh4 – yAtg7 C terminal + yAtg8 (mutant) + ATP
  • Autophagy-related protein 7+10
    • 4gsk – yAtg7 (mutant) + yAtg10 (mutant)
  • Autophagy-related protein 8+19
    • 2zpn – yAtg8 + yAtg19 peptide
  • Autophagy-related protein 8+32
    • 3vxw – yAtg8 + yAtg32 peptide
  • Autophagy-related protein 13+101
    • 4yk8 – Atg13 + Atg101 – fission yeast
  • Autophagy-related protein 17+29+31
    • 4hpq – yAtg17 peptide + yAtg29 + yAtg31 (mutant)
  • Autophagy-related protein 13+17+29+31
    • 4p1w – yAtg13 + yAtg17 peptide +

ReferencesReferences

  1. Shibutani ST, Saitoh T, Nowag H, Munz C, Yoshimori T. Autophagy and autophagy-related proteins in the immune system. Nat Immunol. 2015 Sep 18;16(10):1014-24. doi: 10.1038/ni.3273. PMID:26382870 doi:http://dx.doi.org/10.1038/ni.3273
  2. Noda NN, Satoo K, Fujioka Y, Kumeta H, Ogura K, Nakatogawa H, Ohsumi Y, Inagaki F. Structural basis of Atg8 activation by a homodimeric E1, Atg7. Mol Cell. 2011 Nov 4;44(3):462-75. PMID:22055191 doi:10.1016/j.molcel.2011.08.035

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