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ABSTRACT: Background
Membrane trafficking is a defining feature of eukaryotic cells, and is essential for the maintenance of organelle homeostasis and identity. We previously identified Scy1-like 1 (Scyl1), a member of the Scy1-like family of catalytically inactive protein kinases, as a high-affinity binding partner of COPI coats. COPI-coated vesicles control Golgi to endoplasmic reticulum trafficking and we observed that disruption of Scyl1 function leads to a decrease in trafficking of the KDEL receptor via the COPI pathway. We reasoned that if Scyl1 plays a major role in COPI trafficking its disruption could influence Golgi homeostasis.Methodology/principal findings
We performed Scyl1 knock down in cultured cells using previously established methods and observed an alteration in G
SUBMITTER: Burman JL
PROVIDER: S-EPMC2832016 | biostudies-literature | 2010 Mar
REPOSITORIES: biostudies-literature