@article{fdi:010080152,
  title = {{SUMO}ylated {SNF}2{PH} promotes variant surface glycoprotein expression in bloodstream trypanosomes},
  author = {{S}aura, {A}. and {I}ribarren, {P}.{A}. and {R}ojas-{B}arros, {D}. and {B}art, {J}ean-{M}athieu and {L}ópez-{F}arfán, {D}. and {A}ndr{\'e}s-{L}eón, {E}. and {V}idal-{C}obo, {I}. and {B}oehm, {C}. and {A}lvarez, {V}.{E}. and {F}ield, {M}.{C}. and {N}avarro, {M}.},
  editor = {},
  language = {{ENG}},
  abstract = {{SUMO}ylation is a post-translational modification that positively regulates monoallelic expression of the trypanosome variant surface glycoprotein ({VSG}). {T}he presence of a highly {SUMO}ylated focus associated with the nuclear body, where the {VSG} gene is transcribed, further suggests an important role of {SUMO}ylation in regulating {VSG} expression. {H}ere, we show that {SNF}2{PH}, a {SUMO}ylated plant homeodomain ({PH})-transcription factor, is upregulated in the bloodstream form of the parasite and enriched at the active {VSG} telomere. {SUMO}ylation promotes the recruitment of {SNF}2{PH} to the {VSG} promoter, where it is required to maintain {RNA} polymerase {I} and thus to regulate {VSG} transcript levels. {F}urther, ectopic overexpression of {SNF}2{PH} in insect forms, but not of a mutant lacking the {PH} domain, induces the expression of bloodstream stage-specific surface proteins. {T}hese data suggest that {SNF}2{PH} {SUMO}ylation positively regulates {VSG} monoallelic transcription, while the {PH} domain is required for the expression of bloodstream-specific surface proteins. {T}hus, {SNF}2{PH} functions as a positive activator, linking expression of infective form surface proteins and {VSG} regulation, thereby acting as a major regulator of pathogenicity.},
  keywords = {{AFRIQUE}},
  booktitle = {},
  journal = {{E}mbo {R}eports},
  volume = {20},
  numero = {12},
  pages = {e48029 [18 ]},
  ISSN = {1469-221{X}},
  year = {2019},
  DOI = {10.15252/embr.201948029},
  URL = {https://www.documentation.ird.fr/hor/fdi:010080152},
}