Table 1.

Mass Spectrometric Analysis of Raptor Phosphorylation.

Residues	Peptide Sequence	Phosphorylated Residue(s)	CNT	EC
691–709	NYALPsPATTEGGSLTPVR	S696	−	+
691–716	NYALPSPATTEGGsLTPVRDSPCTPR	S704	−	+
691–709	NYALPSPATTEGGSLtPVR	T706	−	+
691–709	NYALPsPATTEGGSLtPVR	S696 & T706	−	+
719–727	SVSsYGNIR	S722	+	−
790–813	ASsYSSLNSLIGVSFNSVYTQIWR	S792	+	+
850–867	VLDTSSLtQSAPASPTNK	T857	−	+
850–867	VLDTSSLTQsAPASPTNK	S859	+	−
850–867	VLDTSSLTQSAPAsPTNK	S863	+	+
850–867	VLDTSSLTQsAPAsPTNK	S859 & S863	+	+
850–867	VLDTSSLTQSAPASPtNK	T865	−	+
868–894	GVHIHQAGGsPPASSTSSSSLTNDVAK	S877	+	+
868–894	GVHIHQAGGSPPASsTSSSSLTNDVAK	S882	+	−
868–894	GVHIHQAGGSPPASSTSSSsLTNDVAK	S887	+	−

Mouse TA muscles were transfected with FLAG-Raptor. At 7 days post transfection, the muscles were subjected mechanical stimulation via a bout of eccentric contractions (EC), or the control condition, and collected 40 min later. The samples were then subjected to immunoprecipitation for the FLAG tag and resolved on a SDS-PAGE gel. The FLAG-Raptor band was cut-out of the gel, digested with Trypsin and then submitted for LC/MS/MS analysis as detailed in the methods. Fourteen different sites of phosphorylation were identified in control and EC samples and are summarized in the table. + indicates that the phosphorylated peptide was detected during the mass spectrometric analysis of the respective sample and the lower-case letter signifies the phosphorylated amino acid.