The GARP complex is required for cellular sphingolipid homeostasis.
Boston, United States. In Elife, 2014
A GARP complex mutation analogous to a VPS53 allele causing progressive cerebello-cerebral atrophy type 2 (PCCA2) in humans exhibits similar, albeit weaker, phenotypes in yeast, providing mechanistic insights into disease pathogenesis.
VPS53 mutations cause progressive cerebello-cerebral atrophy type 2 (PCCA2).
Beersheba, Israel. In J Med Genet, 2014
Whole exome sequencing identified only two mutations within this locus, which were common to the affected individuals: compound heterozygous mutations in VPS53, segregating as expected for autosomal recessive heredity within all four families, and common in Moroccan Jews (∼1:37 carrier rate).
Transport according to GARP: receiving retrograde cargo at the trans-Golgi network.
Bethesda, United States. In Trends Cell Biol, 2011
X-ray crystallography of the Vps53 and Vps54 subunits of GARP has revealed that this complex is structurally related to other tethering factors such as the exocyst, the conserved oligomeric Golgi (COG) and Dsl1 (dependence on SLY1-20) complexes, indicating that they all might work by a similar mechanism.
Remote homology between Munc13 MUN domain and vesicle tethering complexes.
Dallas, United States. In J Mol Biol, 2009
We found weak yet significant sequence similarities between the MUN domain and a set of protein subunits from several related vesicle tethering complexes, such as Sec6 from the exocyst complex and Vps53 from the Golgi-associated retrograde protein complex.