High impact information on AXL2

• Bud5 also physically interacts with Axl2/Bud10, a transmembrane glycoprotein, suggesting that a receptor-like transmembrane protein recruits a GDP/GTP exchange factor to connect an intrinsic spatial signal to oriented cell growth [1].
• Genetic analysis indicates that AXL2 falls into the same epistasis group as BUD3 [2].
• One such gene, AXL2, has been characterized in detail. axl2 cells are defective in bud site selection in haploid cells and bud in a bipolar fashion [2].
• Selection of axial growth sites in yeast requires Axl2p, a novel plasma membrane glycoprotein [2].
• Overexpression of AXL2 can partially restore proper bud-site selection to pmt4 mutants [3].

Biological context of AXL2

• Towards the end of the cell cycle, the localization of Bud10p refines to a tight double ring which splits at cytokinesis into two single rings, one in each progeny cell [4].

Anatomical context of AXL2

• We suggest that Axl2p acts as an anchor in the plasma membrane that helps direct new growth components and/or polarity establishment components to the cortical axial budding site [2].
• Subcellular fractionations confirm that Bud10p is associated with membranes [4].
• Deletion of ERV14 causes a defect in polarized growth because Axl2p, a transmembrane secretory protein, accumulates in the endoplasmic reticulum and is not delivered to its site of function on the cell surface [5].
• Clusters of Bud10p at the mother-bud neck formed in response to Bud3p (and possibly to an extracellular cue, such as a component of the cell wall), might facilitate the docking of downstream components that direct polarization of the cytoskeleton [4].

Associations of AXL2 with chemical compounds

• Three of the four known proteins required for axial budding, Bud3p, Bud4p, and Axl2p, were expressed and localized appropriately in glucose-limiting conditions [6].

Physical interactions of AXL2

• Axl2p interacts with Cdc42p and other polarity-establishment proteins, and it regulates septin organization in late G1 independently of its role in polarity-axis determination [7].

Other interactions of AXL2

• Because Bud10p contains a large extracellular domain, it is possible that Bud10p functions in a manner analogous to an extracellular matrix receptor [4].

References