The embodiments herein generally relate to a novel finding wherein eight amino-acid sequence in s6 kinase 1 is implicated to exclusively mediate insulin response. Description of the Related Art [002] The general perception of insulin signaling has been to propagate its response through mTORC1 pathway. Other reports, including ours, have established the involvement of mTORC2 as well in this interplay to perhaps provide a link that connects metabolic dynamics with cellular translation. We have, over the years, identified sequence motifs through which mTORC1 and mTORC2 responses can selectively be modulated independent of insulin response. [003] mTOR (a mammalian target of rapamycin) is a major regulator of cell growth and proliferation in response to growth factors/insulin and cellular nutrients. mTOR is a central regulator of ribosome binding to mRNA, which is the rate-limiting step for translating mRNA into protein. mTOR exists in the form of two multiprotein complexes- a rapamycin sensitive mTOR complex 1 (mTORC1) and a rapamycin resistant mTOR complex 2 (mTORC2). Both the complexes have been collectively implicated to participate in mediating growth factor/insulin response. However, no evidence has till date been put forward that suggest insulin/growth factor response is an independent step that requires prior inputs from mTORC1 and mTORC2 on to S6 Kinase 1 (S6K1). S6K1 exists in two isoforms (αI and αII isoforms), which are transcribed from a single gene by alternative mRNA splicing. The αI isoform containing 525 amino acid residues, has an additional 23 amino acid residue segment at N-terminus that encodes a nuclear localization motif. On the other hand, αII isoform having 502 amino-acid residues, is cytoplasmic and starts at a Met residue equivalent to Met- 3 24 in the αI isoform. Thereafter, the sequences of both isoforms are identical. From here onward, S6K1 refers to the larger αI isoform. [004] Accordingly, amino acid sufficiency that activates mTORC1 results in phosphorylation of eukaryotic translation initiation factor 4E (eIF4E). Phosphorylated eIF4E engages with TOS-motif of S6K1 to remove its autoinhibition due to carboxy terminus domain. This disinhibition results in engagement of rictor with the catalytic domain of S6K1 for its phosphorylation at T412 (or T389 in αII isoform of S6K1) and its activation. [005] The response of insulin has so far been masked by these two steps and therefore isolated. The identification of eight amino acid stretch herein highlights that insulin response is over and above the regulatory role played by mTORC1 or mTORC2.