During starvation, autophagy degrades cytoplasmic constituents including organelles such as ER and mitochondria.It remains unclear to what extent and how organelle cargos impose special requirements on the autophagy machinery.In the budding yeast, Atg20 and Atg24,which contain the PX domain and the BAR domain, have been implicated in organelle autophagy.Here we show that their fission yeast homologs, Atg20, Atg24, and Atg24b,participate in starvation-induced autophagy of ER and mitochondria.We found that these proteins accumulate on the pre-autophagosome structure (PAS) in a manner dependent on the autophagy-associated PI3K complex.Loss of any one of these three proteins does not cause an obvious autophagy defect, whereas the simultaneous loss of Atg24 and Atg20, or Atg24 and Atg24b, results in significant impairment of the autophagy of ER and mitochondria, but little reduction of bulk autophagy.Atg20 can interact with Atg24b, and Atg24 can self-associate.Thus, we propose that either a hetero-oligomer of Atg20 and Atg24b, or an Atg24 homo-oligomer, is sufficient for organelle autophagy in fission yeast.Our study suggests that Atg20 and Atg24 family proteins may be universally important for organelle autophagy.