High impact information on BET2

• Therefore MAD2 and BET2 gene products may physically interact to form a geranylgeranyl transferase complex [1].
• We have shown that Bet2p is a component of the yeast GGTase-II (refs 6, 12) that geranylgeranylates Ypt1p, a small GTP-binding protein that mediates transport from the endoplasmic reticulum to the Golgi complex [2].
• DNA sequence analysis has revealed that Bet2 is homologous to Dpr1 (Ram1), an essential component of a protein prenyltransferase that modifies Ras, enabling it to attach to membranes [3].
• We propose that Bet2 modifies Ypt1 and Sec4 in an analogous manner [3].
• The new mutants, bet1 and bet2, are temperature sensitive for growth and protein transport [4].

Biological context of BET2

• Comparisons of the amino acid sequences suggest that the proteins encoded by the Saccharomyces cerevisiae genes MAD2 and BET2 are the yeast counterparts of the mammalian Rab GG transferase alpha and beta subunits, respectively [5].
• Mutations in the catalytic subunits of the yeast GGTase-II (Bet2p/Mad2p) disrupt the membrane attachment of Ypt1p and Sec4p and this in turn blocks membrane traffic [6].

Associations of BET2 with chemical compounds

• Bet2p forms a complex with Mad2p that appears to bind geranylgeranyl pyrophosphate, but not farnesyl pyrophosphate [2].

Other interactions of BET2

• An analysis of BET1, BET2, and BOS1. Three factors mediating ER to Golgi transport in yeast [7].

References