WW domains and retrovirus budding

Garnier, Lucie; Wills, John W.; Verderame, Michael F.; Sudol, Marius

doi:10.1038/381744a0

Cited by 113 publications

(102 citation statements)

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“…In addition to their biological activity in budding, an intriguing characteristic of the L-domains is their ability to mediate interactions with cellular proteins (22,27,33). It has been hypothesized that L-domain activity may be dependent on a virus-host interaction(s), perhaps at the budding site on the plasma membrane (22,26,27,33).…”

Section: Discussionmentioning

confidence: 99%

“…One characteristic of these PY motifs was their ability to mediate interactions with select WW-domains of cellular proteins (22,27). To determine whether the VP40 PY motif could mediate interactions with WW domains of cellular proteins, Western-ligand blotting assays were used.…”

Section: Py Motif Of Vp40 Interacts With Cellular Ww Domainsmentioning

confidence: 99%

“…In addition to their role in virus budding, L-domains have been shown to mediate interactions with cellular proteins that may facilitate or promote virus budding (22,27,33,36). For example, the PY motifs within the RSV Gag, VSV M, and rabies virus M proteins were shown to interact with WW-domains of specific cellular proteins (22,27).…”

mentioning

confidence: 99%

“…For example, the PY motifs within the RSV Gag, VSV M, and rabies virus M proteins were shown to interact with WW-domains of specific cellular proteins (22,27). WW-domains are modular, hydrophobic domains found in a wide variety of cellular proteins, and these domains are classified as types I-IV, depending on the core sequence of the ligand (e.g., PPxY) with which they interact (36)(37)(38)(39)(40)(41)(42).…”

mentioning

confidence: 99%

“…Wills et al were the first to demonstrate that a similar proline-rich motif (PPxY or PY motif, where P ϭ proline, x ϭ any amino acid, and Y ϭ tyrosine) within the p2b region of the Gag polyprotein of Rous sarcoma virus (RSV) plays a critical role during a late stage of virus budding (22)(23)(24)(25). As a result, the PY motif of RSV Gag was termed the L-domain for late budding domain (24,25).…”

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confidence: 99%

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A PPxY motif within the VP40 protein of Ebola virus interacts physically and functionally with a ubiquitin ligase: Implications for filovirus budding

Harty

Brown

Wang

et al. 2000

Proc. Natl. Acad. Sci. U.S.A.

422

465

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VP40, the putative matrix protein of both Ebola and Marburg viruses, possesses a conserved proline-rich motif (PY motif) at its N terminus. We demonstrate that the VP40 protein can mediate its own release from mammalian cells, and that the PY motif is important for this self-exocytosis (budding) function. In addition, we used Western-ligand blotting to demonstrate that the PY motif of VP40 can mediate interactions with specific cellular proteins that have type I WW-domains, including the mammalian ubiquitin ligase, Nedd4. Single point mutations that disrupted the PY motif of VP40 abolished the PY͞WW-domain interactions. Significantly, the full-length VP40 protein was shown to interact both physically and functionally with full-length Rsp5, a ubiquitin ligase of yeast and homolog of Nedd4. The VP40 protein was multiubiquitinated by Rsp5 in a PY-dependent manner in an in vitro ubiquitination assay. These data demonstrate that the VP40 protein of Ebola virus possesses a PY motif that is functionally similar to those described previously for Gag and M proteins of specific retroviruses and rhabdoviruses, respectively. Last, these studies imply that VP40 likely plays an important role in filovirus budding, and that budding of retroviruses, rhabdoviruses, and filoviruses may proceed via analogous mechanisms.

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Section: Discussionmentioning

confidence: 99%

Section: Py Motif Of Vp40 Interacts With Cellular Ww Domainsmentioning

confidence: 99%

mentioning

confidence: 99%