Abstract:
:Mammalian, or mechanistic, target of rapamycin complex 2 (mTORC2) regulates a variety of vital cellular processes, and its aberrant functioning is often associated with various diseases. Rictor is a peculiar and distinguishing mTORC2 component playing a pivotal role in controlling its assembly and activity. Among extant organisms, Rictor is conserved from unicellular eukaryotes to metazoans. We replaced two distinct, but conserved, glycine residues in both the Dictyostelium piaA gene and its human ortholog, RICTOR The two conserved residues are spaced ∼50 amino acids apart, and both are embedded within a conserved region falling in between the Ras-GEFN2 and Rictor-_V domains. The effects of point mutations on the mTORC2 activity and integrity were assessed by biochemical and functional assays. In both cases, these equivalent point mutations in the mammalian RICTOR and DictyosteliumpiaA gene impaired mTORC2 activity and integrity. Our data indicate that the two glycine residues are essential for the maintenance of mTORC2 activity and integrity in organisms that appear to be distantly related, suggesting that they have a evolutionarily conserved role in the assembly and proper mTORC2 functioning.
journal_name
J Cell Scijournal_title
Journal of cell scienceauthors
Pergolizzi B,Panuzzo C,Ali MS,Lo Iacono M,Levra Levron C,Ponzone L,Prelli M,Cilloni D,Calautti E,Bozzaro S,Bracco Edoi
10.1242/jcs.236505subject
Has Abstractpub_date
2019-11-14 00:00:00issue
22eissn
0021-9533issn
1477-9137pii
jcs.236505journal_volume
132pub_type
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