Translational and Posttranslational Dynamics in a Model Peptidergic System

Soledad Barez-Lopez; Andre D S Mecawi; Natasha R Bryan; Audrys G Pauza; Victor J  Duque; Benjamin T Gillard; David Murphy; Michael P Greenwood

doi:10.1016/j.mcpro.2023.100544

Translational and Posttranslational Dynamics in a Model Peptidergic System

Soledad Barez-Lopez, Andre D S Mecawi, Natasha R Bryan, Audrys G Pauza, Victor J Duque, Benjamin T Gillard, David Murphy, Michael P Greenwood^*

^*Corresponding author for this work

Research output: Contribution to journal › Article (Academic Journal) › peer-review

3 Citations (Scopus)

Abstract

The cell bodies of hypothalamic magnocellular neurones are densely packed in the hypothalamic supraoptic nucleus whereas their axons project to the anatomically discrete posterior pituitary gland. We have taken advantage of this unique anatomical structure to establish proteome and phosphoproteome dynamics in neuronal cell bodies and axonal terminals in response to physiological stimulation. We have found that proteome and phosphoproteome responses to neuronal stimulation are very different between somatic and axonal neuronal compartments, indicating the need of each cell domain to differentially adapt. In particular, changes in the phosphoproteome in the cell body are involved in the reorganisation of the cytoskeleton and in axonal terminals the regulation of synaptic and secretory processes. We have identified that prohormone precursors including vasopressin and oxytocin are phosphorylated in axonal terminals and are hyperphosphorylated following stimulation. By multi-omic integration of transcriptome and proteomic data we identify changes to proteins present in afferent inputs to this nucleus.

Original language	English
Article number	100544
Pages (from-to)	100544
Number of pages	1
Journal	Molecular and Cellular Proteomics
Volume	22
Issue number	5
DOIs	https://doi.org/10.1016/j.mcpro.2023.100544
Publication status	Published - 16 May 2023

Bibliographical note

Funding Information:
The authors gratefully acknowledge Dr Kate J. Heesom and Dr Philip A. Lewis from the University of Bristol Proteomics Facility for their support and assistance. We also thank the Wolfson Bioimaging Facility. This research was supported by grants from the Biotechnology and Biological Sciences Research Council (BBSRC; BB/R016879/1) to D. M., S. B. L., and M. P. G., from the Leverhulme Trust (RPG-2017-287) to D. M. and M. P. G., from The Royal Society (Newton Advanced Fellowship, NAF\R2\202118) to D. M. and A. S. M., and from the São Paulo Research Foundation (FAPESP; 2019/ 27581-0) to A. S. M. Students were supported by grants from the Biotechnology and Biological Sciences Research CouncilSWBio DTP programme (BBSRC BB/M009122/1) to B. T .G., the British Heart Foundation to A. G. P (BHF FS/17/60/33474) and to N.B. (FS/4yPhD/F/21/34162), and FAPESP to V. J. D (2021/14426-6).

Funding Information:
supported by grants from the Biotechnology and Biological Sciences Research Council (BBSRC; BB/R016879/1) to D. M., S. B. L., and M. P. G., from the Leverhulme Trust (RPG-2017-287) to D. M. and M. P. G., from The Royal Society (Newton Advanced Fellowship, NAF\R2\202118) to D. M. and A. S. M., and from the São Paulo Research Foundation (FAPESP; 2019/ 27581-0) to A. S. M. Students were supported by grants from the Biotechnology and Biological Sciences Research Council-SWBio DTP programme (BBSRC BB/M009122/1) to B. T .G., the British Heart Foundation to A. G. P (BHF FS/17/60/33474) and to N.B. (FS/4yPhD/F/21/34162), and FAPESP to V. J. D (2021/14426-6).

Publisher Copyright:
© 2023 THE AUTHORS. Published by Elsevier Inc on behalf of American Society for Biochemistry and Molecular Biology.

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title = "Translational and Posttranslational Dynamics in a Model Peptidergic System",

abstract = "The cell bodies of hypothalamic magnocellular neurones are densely packed in the hypothalamic supraoptic nucleus whereas their axons project to the anatomically discrete posterior pituitary gland. We have taken advantage of this unique anatomical structure to establish proteome and phosphoproteome dynamics in neuronal cell bodies and axonal terminals in response to physiological stimulation. We have found that proteome and phosphoproteome responses to neuronal stimulation are very different between somatic and axonal neuronal compartments, indicating the need of each cell domain to differentially adapt. In particular, changes in the phosphoproteome in the cell body are involved in the reorganisation of the cytoskeleton and in axonal terminals the regulation of synaptic and secretory processes. We have identified that prohormone precursors including vasopressin and oxytocin are phosphorylated in axonal terminals and are hyperphosphorylated following stimulation. By multi-omic integration of transcriptome and proteomic data we identify changes to proteins present in afferent inputs to this nucleus. ",

author = "Soledad Barez-Lopez and Mecawi, {Andre D S} and Bryan, {Natasha R} and Pauza, {Audrys G} and Duque, {Victor J} and Gillard, {Benjamin T} and David Murphy and Greenwood, {Michael P}",

note = "Funding Information: The authors gratefully acknowledge Dr Kate J. Heesom and Dr Philip A. Lewis from the University of Bristol Proteomics Facility for their support and assistance. We also thank the Wolfson Bioimaging Facility. This research was supported by grants from the Biotechnology and Biological Sciences Research Council (BBSRC; BB/R016879/1) to D. M., S. B. L., and M. P. G., from the Leverhulme Trust (RPG-2017-287) to D. M. and M. P. G., from The Royal Society (Newton Advanced Fellowship, NAF\R2\202118) to D. M. and A. S. M., and from the S{\~a}o Paulo Research Foundation (FAPESP; 2019/ 27581-0) to A. S. M. Students were supported by grants from the Biotechnology and Biological Sciences Research CouncilSWBio DTP programme (BBSRC BB/M009122/1) to B. T .G., the British Heart Foundation to A. G. P (BHF FS/17/60/33474) and to N.B. (FS/4yPhD/F/21/34162), and FAPESP to V. J. D (2021/14426-6). Funding Information: supported by grants from the Biotechnology and Biological Sciences Research Council (BBSRC; BB/R016879/1) to D. M., S. B. L., and M. P. G., from the Leverhulme Trust (RPG-2017-287) to D. M. and M. P. G., from The Royal Society (Newton Advanced Fellowship, NAF\R2\202118) to D. M. and A. S. M., and from the S{\~a}o Paulo Research Foundation (FAPESP; 2019/ 27581-0) to A. S. M. Students were supported by grants from the Biotechnology and Biological Sciences Research Council-SWBio DTP programme (BBSRC BB/M009122/1) to B. T .G., the British Heart Foundation to A. G. P (BHF FS/17/60/33474) and to N.B. (FS/4yPhD/F/21/34162), and FAPESP to V. J. D (2021/14426-6). Publisher Copyright: {\textcopyright} 2023 THE AUTHORS. Published by Elsevier Inc on behalf of American Society for Biochemistry and Molecular Biology.",

year = "2023",

month = may,

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doi = "10.1016/j.mcpro.2023.100544",

language = "English",

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TY - JOUR

T1 - Translational and Posttranslational Dynamics in a Model Peptidergic System

AU - Barez-Lopez, Soledad

AU - Mecawi, Andre D S

AU - Bryan, Natasha R

AU - Pauza, Audrys G

AU - Duque, Victor J

AU - Gillard, Benjamin T

AU - Murphy, David

AU - Greenwood, Michael P

N1 - Funding Information: The authors gratefully acknowledge Dr Kate J. Heesom and Dr Philip A. Lewis from the University of Bristol Proteomics Facility for their support and assistance. We also thank the Wolfson Bioimaging Facility. This research was supported by grants from the Biotechnology and Biological Sciences Research Council (BBSRC; BB/R016879/1) to D. M., S. B. L., and M. P. G., from the Leverhulme Trust (RPG-2017-287) to D. M. and M. P. G., from The Royal Society (Newton Advanced Fellowship, NAF\R2\202118) to D. M. and A. S. M., and from the São Paulo Research Foundation (FAPESP; 2019/ 27581-0) to A. S. M. Students were supported by grants from the Biotechnology and Biological Sciences Research CouncilSWBio DTP programme (BBSRC BB/M009122/1) to B. T .G., the British Heart Foundation to A. G. P (BHF FS/17/60/33474) and to N.B. (FS/4yPhD/F/21/34162), and FAPESP to V. J. D (2021/14426-6). Funding Information: supported by grants from the Biotechnology and Biological Sciences Research Council (BBSRC; BB/R016879/1) to D. M., S. B. L., and M. P. G., from the Leverhulme Trust (RPG-2017-287) to D. M. and M. P. G., from The Royal Society (Newton Advanced Fellowship, NAF\R2\202118) to D. M. and A. S. M., and from the São Paulo Research Foundation (FAPESP; 2019/ 27581-0) to A. S. M. Students were supported by grants from the Biotechnology and Biological Sciences Research Council-SWBio DTP programme (BBSRC BB/M009122/1) to B. T .G., the British Heart Foundation to A. G. P (BHF FS/17/60/33474) and to N.B. (FS/4yPhD/F/21/34162), and FAPESP to V. J. D (2021/14426-6). Publisher Copyright: © 2023 THE AUTHORS. Published by Elsevier Inc on behalf of American Society for Biochemistry and Molecular Biology.

PY - 2023/5/16

Y1 - 2023/5/16

N2 - The cell bodies of hypothalamic magnocellular neurones are densely packed in the hypothalamic supraoptic nucleus whereas their axons project to the anatomically discrete posterior pituitary gland. We have taken advantage of this unique anatomical structure to establish proteome and phosphoproteome dynamics in neuronal cell bodies and axonal terminals in response to physiological stimulation. We have found that proteome and phosphoproteome responses to neuronal stimulation are very different between somatic and axonal neuronal compartments, indicating the need of each cell domain to differentially adapt. In particular, changes in the phosphoproteome in the cell body are involved in the reorganisation of the cytoskeleton and in axonal terminals the regulation of synaptic and secretory processes. We have identified that prohormone precursors including vasopressin and oxytocin are phosphorylated in axonal terminals and are hyperphosphorylated following stimulation. By multi-omic integration of transcriptome and proteomic data we identify changes to proteins present in afferent inputs to this nucleus.

AB - The cell bodies of hypothalamic magnocellular neurones are densely packed in the hypothalamic supraoptic nucleus whereas their axons project to the anatomically discrete posterior pituitary gland. We have taken advantage of this unique anatomical structure to establish proteome and phosphoproteome dynamics in neuronal cell bodies and axonal terminals in response to physiological stimulation. We have found that proteome and phosphoproteome responses to neuronal stimulation are very different between somatic and axonal neuronal compartments, indicating the need of each cell domain to differentially adapt. In particular, changes in the phosphoproteome in the cell body are involved in the reorganisation of the cytoskeleton and in axonal terminals the regulation of synaptic and secretory processes. We have identified that prohormone precursors including vasopressin and oxytocin are phosphorylated in axonal terminals and are hyperphosphorylated following stimulation. By multi-omic integration of transcriptome and proteomic data we identify changes to proteins present in afferent inputs to this nucleus.

UR - http://dx.doi.org/10.1016/j.mcpro.2023.100544

U2 - 10.1016/j.mcpro.2023.100544

DO - 10.1016/j.mcpro.2023.100544

M3 - Article (Academic Journal)

C2 - 37030596

SN - 1535-9476

VL - 22

SP - 100544

JO - Molecular and Cellular Proteomics

JF - Molecular and Cellular Proteomics

IS - 5

M1 - 100544

ER -

Translational and Posttranslational Dynamics in a Model Peptidergic System

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