Neutral lipid metabolism enzymes and LD (Lipid Droplets)-associated proteins

Range Table - link
Organism Budding yeast Saccharomyces cerevisiae
Reference Kohlwein SD, Veenhuis M, van der Klei IJ. Lipid droplets and peroxisomes: key players in cellular lipid homeostasis or a matter of fatstore 'em up or burn 'em down. Genetics. 2013 Jan193(1):1-50. doi: 10.1534/genetics.112.143362. pp.6-7 table 1PubMed ID23275493
Primary Source See pointers to refs at bottom of table
Comments P.15 left column 3rd paragraph: "Targeting of proteins to LDs-Unlike other proteins targeted to organelles, LD-associated proteins apparently do not harbor targeting consensus sequences as determined by primary structure comparison of LD-associated proteins. However, a common feature appears to be the presence of hydrophobic domains, although exceptions exist (Leber et al. 1998 Mullner et al. 2004 Grillitsch et al. 2011). As shown in Table 1, several of the LD-associated proteins contain even one or two (predicted) transmembrane domains, which appear to be incompatible with the generally accepted view that the LD surface is covered by a phospholipid monolayer. Thus it is unclear how these extended stretches of hydrophobic amino acids are accommodated in the LD surface layer. Also, numerous LD proteins lack hydrophobic stretches indicative of membrane-anchoring sequences altogether (Table 1), suggesting that their interaction with LDs may be indirect and through the interaction with LD-anchored proteins."
Entered by Uri M
ID 113130