Human immunodeficiency virus-1 Tat protein interacts with distinct proteasomal alpha and beta subunits.

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Apcher GS, Heink S, Zantopf D, Kloetzel PM, Schmid HP, Mayer RJ, Kruger E

Human immunodeficiency virus-1 Tat protein interacts with distinct proteasomal alpha and beta subunits.

FEBS Lett. 2003 Oct 9;553(1-2):200-4.

PubMed ID
14550573 [ View in PubMed
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Abstract

The human immunodeficiency virus-1 (HIV-1) Tat protein was previously reported to compete the association of PA28 regulator with the alpha rings of the 20S proteasome and to inhibit its peptidase activity. However, the distinct interaction sites within the proteasome complex remained to be determined. Here we show that HIV-1 Tat binds to alpha4 and alpha7, six beta subunits of the constitutive 20S proteasome and the interferon-gamma-inducible subunits beta2i and beta5i. A Tat-proteasome interaction can also be demonstrated in vivo and leads to inhibition of proteasomal activity. This indicates that Tat can modulate or interfere with cellular proteasome function by specific interaction with distinct proteasomal subunits.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
Proteasome subunit beta type-1P20618Details
Proteasome subunit beta type-5P28074Details
Proteasome subunit beta type-2P49721Details
Proteasome subunit alpha type-3P25788Details
Proteasome subunit alpha type-7O14818Details
Proteasome subunit beta type-3P49720Details
Proteasome subunit beta type-4P28070Details
Proteasome subunit beta type-6P28072Details
Proteasome subunit beta type-7Q99436Details
Proteasome subunit beta type-9P28065Details
Proteasome subunit beta type-10P40306Details
Proteasome subunit beta type-8P28062Details