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15-141 The endoplasmic reticulum-associated mRNA-binding protein ERBP1

ABSTRACT: Kinetoplastids rely heavily on post-transcriptional mechanisms for control of gene expression, and on RNA-binding proteins that regulate mRNA splicing, translation and decay. Trypanosoma brucei ERBP1 (Tb927.10.14150) and ERBP2 (Tb927.9.9550) were previously identified as mRNA binding proteins that lack canonical RNA-binding domains. We here show that ERBP1 is associated with the endoplasmic reticulum, like ERBP2, and that the two proteins interact in vivo. Loss of ERBP1 from bloodstream-form T. brucei initially resulted in a growth defect but proliferation was restored after more prolonged cultivation. Results from a pull-down of tagged ERBP1 suggest that it preferentially binds to ribosomal protein mRNAs. The ERBP1 sequence resembles that of Saccharomyces cerevisiae Bfr1, which also localises to the endoplasmic reticulum and binds to ribosomal protein mRNAs. However, unlike Bfr1, ERBP1 does not bind to mRNAs encoding secreted proteins, and it is also not recruited to stress granules after starvation.

INSTRUMENT(S): LTQ Orbitrap

ORGANISM(S): Trypanosoma Brucei

DISEASE(S): Trypanosomiasis

SUBMITTER: Thomas Ruppert

LAB HEAD: Thomas Ruppert

PROVIDER: PXD016106 | Pride | 2020-01-16

REPOSITORIES: Pride

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			Action	DRS
	X-15-141-01-02-03.mzid_X-15-141-01-02-03.MGF	Mzid
	X-15-141-010203.msf	Msf
	X-15-141-010203.raw	Raw
	X-15-141-013-14-15.mzid_X-15-141-013-14-15.MGF	Mzid
	X-15-141-0131415.raw	Raw

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The endoplasmic reticulum-associated mRNA-binding protein ERBP1 from Trypanosoma brucei

Project description:Kinetoplastids rely heavily on post-transcriptional mechanisms for control of gene expression, and on RNA-binding proteins that regulate mRNA splicing, translation and decay. Trypanosoma brucei ERBP1 (Tb927.10.14150) and ERBP2 (Tb927.9.9550) were previously identified as mRNA binding proteins that lack canonical RNA-binding domains. We here show that ERBP1 is associated with the endoplasmic reticulum, like ERBP2, and that the two proteins interact in vivo. Loss of ERBP1 from bloodstream-form T. brucei initially resulted in a growth defect but proliferation was restored after more prolonged cultivation. Results from a pull-down of tagged ERBP1 suggest that it preferentially binds to ribosomal protein mRNAs. The ERBP1 sequence resembles that of Saccharomyces cerevisiae Bfr1, which also localises to the endoplasmic reticulum and binds to ribosomal protein mRNAs. However, unlike Bfr1, ERBP1 does not bind to mRNAs encoding secreted proteins, and it is also not recruited to stress granules after starvation.

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Altered mitochondria-associated ER membranes (MAM) function shifts mitochondrial metabolism in amyotrophic lateral sclerosis (ALS)- BioID Data

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Altered mitochondria-associated ER membranes (MAM) function shifts mitochondrial metabolism in amyotrophic lateral sclerosis (ALS)

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Tankyrase-1regulates RBP-mediated mRNA turnover to promotemuscle fiber formation.

Project description:Poly(ADP-ribosylation)(PARylation)is apost-translational modification mediated by asubset of ADP-ribosyl transferases (ARTs). Although PARylation-inhibition based therapies areconsidered as an avenue to combat debilitating diseases such as cancerand myopathies, the roleof thismodificationinphysiological processes such ascell differentiation remainsunclear. Here we showthat Tankyrase1 (TNKS1), aPARylating ART, plays a major role in myogenesis, a vital process known to drivemuscle fiber formation and regeneration.Althoughallbona fidePARPs are expressed in muscle cells, experiments using siRNA-mediated knockdownor pharmacological inhibitionshow thatTKNS1 is the enzyme responsible ofcatalyzing PARylation during myogenesis. Via this activity,TKNS1controlsthe turnoverof mRNAs encoding myogenic regulatory factors such as nucleophosmin(NPM) and myogenin.TKNS1 mediates these effectsby targeting RNA-binding proteinssuch as Human Antigen R (HuR). HuR harbors a conserved TNKS-binding motif (TBM), the mutation of which not only prevents theassociation of HuR with TKNS1 anditsPARylation, but also precludes HuR from regulating the turnover of NPMand myogeninmRNAsas well as from promoting myogenesis. Therefore, our data uncovera new role forTNKS1as akeymodulator of RBP-mediated post transcriptionaleventsrequired for vitalprocesses suchasmyogenesis.

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RIP-Seq of HnRNPF/H in Trypanosoma brucei bloodstream forms

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