Proadrenomedullin N-terminal 20 peptide increases kinesin's velocity both in vitro and in vivo

Endocrinology
Ignacio M Larráyoz, Alfredo Martínez

Abstract

Intracellular cargo transport relies on microtubules and motor proteins such as kinesins and dyneins. Currently we have ample knowledge of the mechanisms by which motor proteins propel themselves along the microtubules, but little is known about intracellular factors that regulate motor speed. Here we show that proadrenomedullin N-terminal 20 peptide (PAMP) increases kinesin velocity and ATP consumption in a dose-dependent manner, using a variety of human kinesins. Structure-activity studies found that the terminal amide of PAMP is required for modulating kinesin activity and that the smallest peptide fragment retaining this role is PAMP₁₂₋₂₀. On the other hand, peptide fragments as small as PAMP₁₈₋₂₀ maintained the ability of delaying tubulin polymerization, another function previously described for PAMP, indicating that these two activities depend on different regions of the molecule. To demonstrate that these observations are also relevant in vivo, hippocampal neurons were isolated from mice lacking the gene coding for PAMP and from wild type littermates. Intravital stains followed by time-lapse microscopy analysis revealed that mitochondrial speed inside neurons lacking PAMP was significantly slower than in cells expressing...Continue Reading

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Citations

Mar 31, 2018·Molecular Neurobiology·Hilda FerreroMaría J Ramírez
Sep 4, 2017·Molecular Neurobiology·Hilda FerreroMaría J Ramírez
Dec 1, 2017·Frontiers in Molecular Neuroscience·Ignacio M LarrayozAlfredo Martínez
Apr 20, 2018·Molecular Neurobiology·Hilda FerreroFrancisco J Gil-Bea

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