Name: Proteomic study in sucrose secreting mutant of cyanobacterium Synechococcus elongatus PCC 7942.
Keywords: Synechococcus elongatus (strain pcc 7942) (anacystis nidulans r2)

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Proteomic study in sucrose secreting mutant of cyanobacterium Synechococcus elongatus PCC 7942.

ABSTRACT: We conducted proteomic analysis of a strain engineered for inducible secretion of sucrose.

INSTRUMENT(S): Q Exactive HF

ORGANISM(S): Synechococcus Elongatus (strain Pcc 7942) (anacystis Nidulans R2)

TISSUE(S): Photosynthetic Cell, Cell Culture

DISEASE(S): Disease Free

SUBMITTER: Amit Singh

LAB HEAD: Dr. Daniel C Ducat

PROVIDER: PXD027430 | Pride | 2022-03-21

REPOSITORIES: Pride

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Project description:Many biological processes involve the mechanistic/mammalian target of rapamycin complex 1 (mTORC1). Thus, the challenge of deciphering mTORC1-mediated functions during normal and pathological states in the central nervous system is steep. Because mTORC1 is at the core of translation, we have investigated mTORC1 function in global and regional protein expression. Activation of mTORC1 has been generally regarded to promote translation. Few but recent works have demonstrated that suppression of mTORC1 can promote local protein synthesis. Moreover, excessive mTORC1 activation during disease states represses basal and activity-induced protein synthesis. To determine the role of mTORC1 activation in protein expression, we have used an unbiased, large scale proteomic approach. We provide evidence that a brief repression of mTORC1 activity in vivo by rapamycin has little affect globally, yet leads to a significant remodeling of synaptic proteins, in particular those proteins that reside in the postsynaptic density (PSD). We have also found that curtailing the activity of mTORC1 bidirectionally alters the expression of proteins associated with epilepsy, Alzheimer’s disease, and autism spectrum disorder (ASD)—neurological disorders that exhibit elevated mTORC1 activity. Through a protein-protein interaction network analysis, we have identified common proteins shared among these mTOR-related diseases. One such protein is Parkinson protein 7 (PARK7) which has been implicated in Parkinson’s disease, yet not associated with epilepsy, AD, or ASD. To verify our finding, we provide evidence that the protein expression of PARK7, including new protein synthesis, is sensitive to mTORC1 inhibition. Using cultured neurons from a mouse model of tuberous sclerosis complex (TSC), a disease that displays both epilepsy and ASD phenotypes and has overactive mTOR signaling, we show that PARK7 protein is elevated in the dendrites. Our work offers a comprehensive view of mTORC1 and its role in regulating regional protein expression in normal and diseased states.

Dataset Information

Proteomic study in sucrose secreting mutant of cyanobacterium Synechococcus elongatus PCC 7942.

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