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Literature summary for 2.4.1.12 extracted from

  • Fugelstad, J.; Brown, C.; Hukasova, E.; Sundqvist, G.; Lindqvist, A.; Bulone, V.
    Functional characterization of the pleckstrin homology domain of a cellulose synthase from the oomycete Saprolegnia monoica (2012), Biochem. Biophys. Res. Commun., 417, 1248-1253.
    View publication on PubMed
Search for more literature for 2.4.1.12

Cloned(Commentary)

Cloned (Comment) Organism
CesA2, expression in Escherichia coli strain BL21(DE3) and in human U2OS osteosarcoma cells as GFP-tagged enzyme using the pCDNA™6.2/GW/C-EmGFP vector Saprolegnia monoica

Localization

Localization Comment Organism GeneOntology No. Textmining
actin filament
-
 Saprolegnia monoica 5884
-
cytoplasm co-localized with F-actin Saprolegnia monoica 5737
-
additional information CesA2 might co-localize with microtubules in vivo Saprolegnia monoica
-
-
nucleolus co-localized with F-actin Saprolegnia monoica 5730
-
nucleoplasm co-localized with F-actin Saprolegnia monoica 5654
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Saprolegnia monoica CesA2 binds in vitro to phosphoinositides, F-actin and microtubules via its PH domain, and co-localizes with F-actin in vivo ?
-
 ?

Organism

Organism UniProt Comment Textmining
Saprolegnia monoica C9WPJ9
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information CesA2 binds in vitro to phosphoinositides, F-actin and microtubules via its PH domain, and co-localizes with F-actin in vivo Saprolegnia monoica ?
-
 ?

Synonyms

Synonyms Comment Organism
cellulose synthase 2
-
 Saprolegnia monoica
CesA2
-
 Saprolegnia monoica

General Information

General Information Comment Organism
evolution SmCesA2PH shares the PPBM motif with several PH domains of human proteins, the SmCesA2 PH domain is similar to the C-terminal PH domain of the human protein TAPP1 Saprolegnia monoica
physiological function the SmCesA2 PH domain binds in vitro to phosphoinositides, F-actin and microtubules, and co-localizes with F-actin in vivo. The SmCesA2 PH domain has a role in the regulation, trafficking and/or targeting of the cell wall synthesizing enzyme Saprolegnia monoica