Collapsin Response Mediator Protein - 2 Hyperphosphorylation: Hallmark for contributing to various Neurodegenerative Disorders

preprint OA: closed
📄 Open PDF Full text JSON View at publisher

Abstract

Structural, electrical, and metabolic alterations in the brain characterize neurodegenerative illnesses, which include Parkinson’s disease (PD), Huntington’s disease (HD), Tardive Dyskinesia (TD), epilepsy, Alzheimer’s disease (AD), and schizophrenia. Five distinct phosphoproteins make up the family of cytosolic proteins known as collapsin response mediator proteins (CRMPs), which are significantly produced throughout the nervous system’s development phase. This implies that CRMPs play a crucial part in directing the proliferation of neurons and the formation of axons. These proteins come in two varieties, one shorter (65 kDa) and the other longer (80 kDa) with N-terminal extensions. They are encoded by five different genes. Increased CRMP expression during central nervous system development is linked to several signaling networks, including the Rho Kinase pathway, glycogen synthase kinase-3 (GSK-3), and cyclin-dependent kinase 5 (CDK-5). These signaling pathways’ hyperphosphorylation of CRMP-2 under pathological circumstances leads to neurodegeneration in a number of neurological diseases. In neurodegenerative illnesses, phosphorylated versions of CRMP-2 impair neuronal polarity and limit axonal development, whereas unphosphorylated forms stimulate microtubule assembly and axonal growth. The focus of this review is on investigating the therapeutic effectiveness of CRMP-2 modulation in the treatment of different neurodegenerative diseases.
Full text 6,916 characters · extracted from preprint-html · click to expand
Collapsin Response Mediator Protein - 2 Hyperphosphorylation: Hallmark for contributing to various Neurodegenerative Disorders | Authorea try { document.documentElement.classList.add('js'); } catch (e) { } var _gaq = _gaq || []; _gaq.push(['_setAccount', 'G-8VDV14Y67G']); _gaq.push(['_trackPageview']); (function() { var ga = document.createElement('script'); ga.type = 'text/javascript'; ga.async = true; ga.src = ('https:' == document.location.protocol ? 'https://ssl' : 'http://www') + '.google-analytics.com/ga.js'; var s = document.getElementsByTagName('script')[0]; s.parentNode.insertBefore(ga, s); })(); Skip to main content Preprints Collections Wiley Open Research IET Open Research Ecological Society of Japan All Collections About About Authorea FAQs Contact Us Quick Search anywhere Search for preprint articles, keywords, etc. Search Search ADVANCED SEARCH SCROLL This is a preprint and has not been peer reviewed. Data may be preliminary. 20 May 2025 V1 Latest version Share on Collapsin Response Mediator Protein - 2 Hyperphosphorylation: Hallmark for contributing to various Neurodegenerative Disorders Authors : Sumit Kumar 0009-0005-6285-6888 , Rupesh Pandey [email protected] , Lubhan Singh , and Aradhana Prajapati Authors Info & Affiliations https://doi.org/10.22541/au.174773019.92030334/v1 234 views 116 downloads Contents Abstract Supplementary Material Information & Authors Metrics & Citations View Options References Figures Tables Media Share Abstract Structural, electrical, and metabolic alterations in the brain characterize neurodegenerative illnesses, which include Parkinson’s disease (PD), Huntington’s disease (HD), Tardive Dyskinesia (TD), epilepsy, Alzheimer’s disease (AD), and schizophrenia. Five distinct phosphoproteins make up the family of cytosolic proteins known as collapsin response mediator proteins (CRMPs), which are significantly produced throughout the nervous system’s development phase. This implies that CRMPs play a crucial part in directing the proliferation of neurons and the formation of axons. These proteins come in two varieties, one shorter (65 kDa) and the other longer (80 kDa) with N-terminal extensions. They are encoded by five different genes. Increased CRMP expression during central nervous system development is linked to several signaling networks, including the Rho Kinase pathway, glycogen synthase kinase-3 (GSK-3), and cyclin-dependent kinase 5 (CDK-5). These signaling pathways’ hyperphosphorylation of CRMP-2 under pathological circumstances leads to neurodegeneration in a number of neurological diseases. In neurodegenerative illnesses, phosphorylated versions of CRMP-2 impair neuronal polarity and limit axonal development, whereas unphosphorylated forms stimulate microtubule assembly and axonal growth. The focus of this review is on investigating the therapeutic effectiveness of CRMP-2 modulation in the treatment of different neurodegenerative diseases. Supplementary Material File (content file.docx) Download 492.79 KB Information & Authors Information Version history V1 Version 1 20 May 2025 Copyright This work is licensed under a Non Exclusive No Reuse License. Keywords cognition gpcr intercellular signaling learning & memory modulation neurodegeneration/neuroprotection Authors Affiliations Sumit Kumar 0009-0005-6285-6888 Swami Vivekanand Subharti University View all articles by this author Rupesh Pandey [email protected] Swami Vivekanand Subharti University View all articles by this author Lubhan Singh Swami Vivekanand Subharti University View all articles by this author Aradhana Prajapati Dr KN Modi Institute of Pharmaceutical Sciences and Research View all articles by this author Metrics & Citations Metrics Article Usage 234 views 116 downloads .FvxKWukQNSOunydq8rnd { width: 100px; } Citations Download citation Sumit Kumar, Rupesh Pandey, Lubhan Singh, et al. Collapsin Response Mediator Protein - 2 Hyperphosphorylation: Hallmark for contributing to various Neurodegenerative Disorders. Authorea . 20 May 2025. DOI: https://doi.org/10.22541/au.174773019.92030334/v1 If you have the appropriate software installed, you can download article citation data to the citation manager of your choice. Simply select your manager software from the list below and click Download. For more information or tips please see 'Downloading to a citation manager' in the Help menu . Format Please select one from the list RIS (ProCite, Reference Manager) EndNote BibTex Medlars RefWorks Direct import Tips for downloading citations document.getElementById('citMgrHelpLink').addEventListener('click', function() { popupHelp(this.href); return false; }); $(".js__slcInclude").on("change", function(e){ if ($(this).val() == 'refworks') $('#direct').prop("checked", false); $('#direct').prop("disabled", ($(this).val() == 'refworks')); }); View Options View options PDF View PDF Figures Tables Media Share Share Share article link Copy Link Copied! Copying failed. Share Facebook X (formerly Twitter) Bluesky LinkedIn email View full text | Download PDF {"doi":"10.22541/au.174773019.92030334/v1","type":"Article"} Now Reading: Share Figures Tables Close figure viewer Back to article Figure title goes here Change zoom level Go to figure location within the article Download figure Toggle share panel Toggle share panel Share Toggle information panel Toggle information panel Go to previous graphic Go to next graphic Go to previous table Go to next table All figures All tables View all material View all material xrefBack.goTo xrefBack.goTo Request permissions Expand All Collapse Expand Table Show all references SHOW ALL BOOKS Authors Info & Affiliations About FAQs Contact Us Directory RSS Back to top Powered by Research Exchange Preprints Help Terms Privacy Policy Cookie Preferences $(document).ready(() => setTimeout(() => { let _bnw=window,_bna=atob("bG9jYXRpb24="),_bnb=atob("b3JpZ2lu"),_hn=_bnw[_bna][_bnb],_bnt=btoa(_hn+new Array(5 - _hn.length % 4).join(" ")); $.get("/resource/lodash?t="+_bnt); },4000)); (function(){function c(){var b=a.contentDocument||a.contentWindow.document;if(b){var d=b.createElement('script');d.innerHTML="window.__CF$cv$params={r:'9fea58e11d231640',t:'MTc3OTI2OTY4Mw=='};var a=document.createElement('script');a.src='/cdn-cgi/challenge-platform/scripts/jsd/main.js';document.getElementsByTagName('head')[0].appendChild(a);";b.getElementsByTagName('head')[0].appendChild(d)}}if(document.body){var a=document.createElement('iframe');a.height=1;a.width=1;a.style.position='absolute';a.style.top=0;a.style.left=0;a.style.border='none';a.style.visibility='hidden';document.body.appendChild(a);if('loading'!==document.readyState)c();else if(window.addEventListener)document.addEventListener('DOMContentLoaded',c);else{var e=document.onreadystatechange||function(){};document.onreadystatechange=function(b){e(b);'loading'!==document.readyState&&(document.onreadystatechange=e,c())}}}})();

Text is read by the "Ask this paper" AI Q&A widget below. Extraction quality varies by source — PMC NXML preserves structure cleanly, OA-HTML may include some navigation residue, and OA-PDF can have broken hyphenation. The publisher copy (via DOI) is the canonical version.

My notes (saved in your browser only)

Ask this paper AI returns verbatim quotes from the full text · source: preprint-html

Answers must be backed by verbatim quotes from this paper's full text. Hallucinated quotes are dropped automatically; if no verbatim passage answers the question, we say so. How this works

Citation neighborhood (no data yet)

We don't have any in-corpus citations linked to this paper yet. This is a recent paper (2025) — citers typically take a year or two to land, and the OpenAlex reference graph may still be filling in.

Source provenance

europepmc
last seen: 2026-05-20T01:45:00.602351+00:00
unpaywall
last seen: 2026-06-13T06:42:57.164913+00:00