{"id":35180,"date":"2026-03-18T12:37:00","date_gmt":"2026-03-18T12:37:00","guid":{"rendered":"https:\/\/www.tun.com\/home\/?p=35180"},"modified":"2026-03-18T16:37:03","modified_gmt":"2026-03-18T16:37:03","slug":"competing-brain-proteins-may-reveal-a-new-root-cause-of-alzheimers","status":"publish","type":"post","link":"https:\/\/www.tun.com\/home\/competing-brain-proteins-may-reveal-a-new-root-cause-of-alzheimers\/","title":{"rendered":"Competing Brain Proteins May Reveal a New Root Cause of Alzheimer\u2019s"},"content":{"rendered":"\n<div class=\"wp-block-group\"><div class=\"wp-block-group__inner-container is-layout-constrained wp-block-group-is-layout-constrained\">\n<div class=\"wp-block-uagb-blockquote uagb-block-e7eb3fc3 uagb-blockquote__skin-border uagb-blockquote__stack-img-none\"><blockquote class=\"uagb-blockquote\"><div class=\"uagb-blockquote__content\">A UC Riverside-led team has found that two hallmark Alzheimer\u2019s proteins compete for the same spots inside brain cells, potentially derailing neurons from within. The work offers a simple, unifying theory that could redirect how scientists design future therapies.<\/div><footer><div class=\"uagb-blockquote__author-wrap uagb-blockquote__author-at-left\"><\/div><\/footer><\/blockquote><\/div>\n\n\n\n<div class=\"wp-block-group is-content-justification-space-between is-nowrap is-layout-flex wp-container-core-group-is-layout-0dfbf163 wp-block-group-is-layout-flex\"><div style=\"font-size:16px;\" class=\"has-text-align-left wp-block-post-author\"><div class=\"wp-block-post-author__content\"><p class=\"wp-block-post-author__name\">The University Network<\/p><\/div><\/div>\n\n\n<div class=\"wp-block-uagb-social-share uagb-social-share__outer-wrap uagb-social-share__layout-horizontal uagb-block-ee584a31\">\n<div class=\"wp-block-uagb-social-share-child uagb-ss-repeater uagb-ss__wrapper uagb-block-ec619ce7\"><span class=\"uagb-ss__link\" data-href=\"https:\/\/www.facebook.com\/sharer.php?u=\" tabindex=\"0\" role=\"button\" aria-label=\"facebook\"><span class=\"uagb-ss__source-wrap\"><span class=\"uagb-ss__source-icon\"><svg xmlns=\"https:\/\/www.w3.org\/2000\/svg\" viewBox=\"0 0 512 512\"><path d=\"M504 256C504 119 393 8 256 8S8 119 8 256c0 123.8 90.69 226.4 209.3 245V327.7h-63V256h63v-54.64c0-62.15 37-96.48 93.67-96.48 27.14 0 55.52 4.84 55.52 4.84v61h-31.28c-30.8 0-40.41 19.12-40.41 38.73V256h68.78l-11 71.69h-57.78V501C413.3 482.4 504 379.8 504 256z\"><\/path><\/svg><\/span><\/span><\/span><\/div>\n\n\n\n<div class=\"wp-block-uagb-social-share-child uagb-ss-repeater uagb-ss__wrapper uagb-block-32d99934\"><span class=\"uagb-ss__link\" data-href=\"https:\/\/twitter.com\/share?url=\" tabindex=\"0\" role=\"button\" aria-label=\"twitter\"><span class=\"uagb-ss__source-wrap\"><span class=\"uagb-ss__source-icon\"><svg xmlns=\"https:\/\/www.w3.org\/2000\/svg\" viewBox=\"0 0 512 512\"><path d=\"M389.2 48h70.6L305.6 224.2 487 464H345L233.7 318.6 106.5 464H35.8L200.7 275.5 26.8 48H172.4L272.9 180.9 389.2 48zM364.4 421.8h39.1L151.1 88h-42L364.4 421.8z\"><\/path><\/svg><\/span><\/span><\/span><\/div>\n\n\n\n<div class=\"wp-block-uagb-social-share-child uagb-ss-repeater uagb-ss__wrapper uagb-block-1d136f14\"><span class=\"uagb-ss__link\" data-href=\"https:\/\/www.linkedin.com\/shareArticle?url=\" tabindex=\"0\" role=\"button\" aria-label=\"linkedin\"><span class=\"uagb-ss__source-wrap\"><span class=\"uagb-ss__source-icon\"><svg xmlns=\"https:\/\/www.w3.org\/2000\/svg\" viewBox=\"0 0 448 512\"><path d=\"M416 32H31.9C14.3 32 0 46.5 0 64.3v383.4C0 465.5 14.3 480 31.9 480H416c17.6 0 32-14.5 32-32.3V64.3c0-17.8-14.4-32.3-32-32.3zM135.4 416H69V202.2h66.5V416zm-33.2-243c-21.3 0-38.5-17.3-38.5-38.5S80.9 96 102.2 96c21.2 0 38.5 17.3 38.5 38.5 0 21.3-17.2 38.5-38.5 38.5zm282.1 243h-66.4V312c0-24.8-.5-56.7-34.5-56.7-34.6 0-39.9 27-39.9 54.9V416h-66.4V202.2h63.7v29.2h.9c8.9-16.8 30.6-34.5 62.9-34.5 67.2 0 79.7 44.3 79.7 101.9V416z\"><\/path><\/svg><\/span><\/span><\/span><\/div>\n<\/div>\n<\/div>\n<\/div><\/div>\n\n\n\n<p>For decades, scientists have chased sticky protein clumps in the brain as the main culprits behind Alzheimer\u2019s disease. Yet drug after drug aimed at clearing those clumps has failed to stop the memory-robbing condition.<\/p>\n\n\n\n<p>New research led by the University of California, Riverside, points to a different, more intimate battle happening inside brain cells themselves \u2014 and it could help explain why so many treatments have come up short.<\/p>\n\n\n\n<p>The study, <a href=\"https:\/\/academic.oup.com\/pnasnexus\/article\/5\/3\/pgag034\/8524397\" target=\"_blank\" rel=\"noopener\" title=\"\">published<\/a> in the journal <em>Proceedings of the National Academy of Sciences Nexus<\/em>, suggests that two hallmark Alzheimer\u2019s proteins, amyloid beta (often called a-beta) and tau, are not just bystanders that pile up in the brain. Instead, they appear to compete for the same crucial job inside neurons, disrupting the cell\u2019s internal transport system from within.<\/p>\n\n\n\n<p>Lead author Ryan Julian, a chemistry professor at UC Riverside, noted that both proteins are central to how doctors diagnose the disease. <\/p>\n\n\n\n<p>\u201cIn addition to having dementia, Alzheimer\u2019s diagnosis requires both a-beta and tau buildup in the brain,\u201d Julian said in a news release. \u201cBut many labs focus on the role of one and ignore the other.\u201d<\/p>\n\n\n\n<p>Amyloid beta and tau have long been at the center of Alzheimer\u2019s research. Amyloid beta tends to form plaques outside neurons, while tau forms tangles inside them. Genetic mutations that boost amyloid beta production are known to cause early-onset Alzheimer\u2019s, which helped cement the idea that amyloid plaques drive the disease.<\/p>\n\n\n\n<p>But there has been a major problem with that theory: Thousands of clinical trials that tried to remove amyloid beta from patients\u2019 brains have largely failed to halt or reverse symptoms. At the same time, scientists have known that tau buildup tracks closely with the progression of dementia, but the exact relationship between tau and amyloid beta has remained murky.<\/p>\n\n\n\n<p>Julian\u2019s team approached the question from a different angle, focusing on what tau normally does in healthy brain cells.<\/p>\n\n\n\n<p>Tau\u2019s main job is to stabilize structures called microtubules. These are tiny, hollow tubes that act like highways inside neurons, carrying nutrients, signaling molecules and other cargo to where they are needed. If microtubules fall apart, neurons struggle to move essential materials, which can threaten their survival and ability to communicate.<\/p>\n\n\n\n<p>When the researchers looked closely at the parts of tau that latch onto microtubules, they noticed something striking: those regions closely resembled amyloid beta in size and structure. That similarity raised a provocative possibility \u2014 that amyloid beta might also be able to bind to microtubules, potentially muscling in on tau\u2019s territory.<\/p>\n\n\n\n<p>To test this, the team tagged amyloid beta with a fluorescent marker and watched how it behaved. When the tagged protein slowed down and its light signal changed, it indicated that amyloid beta had attached to microtubules.<\/p>\n\n\n\n<p>The experiments showed that amyloid beta and tau bind to microtubules with roughly the same strength. In other words, if enough amyloid beta accumulates inside neurons, it can push tau aside.<\/p>\n\n\n\n<p>\u201cOur work shows amyloid beta and tau compete for the same binding sites on microtubules, and that a-beta can prevent tau from functioning correctly,\u201d Julian added.<\/p>\n\n\n\n<p>That competition could be the spark that sets off a cascade of damage. If tau is displaced from microtubules, the internal transport system inside neurons may begin to break down. Starved of proper transport, neurons can falter. Meanwhile, tau that is no longer doing its stabilizing job can start to misbehave, clumping together and drifting into parts of the cell where it does not belong.<\/p>\n\n\n\n<p>This model reframes the familiar plaques and tangles seen in Alzheimer\u2019s brains. Instead of being the initial cause, the study suggests that large aggregates of amyloid beta and tau might be downstream effects of an earlier disruption: the fight for control of microtubules inside neurons.<\/p>\n\n\n\n<p>That idea helps reconcile several puzzling observations. For example, amyloid plaques form outside cells, while tau tangles form inside them. If the real trouble starts when amyloid beta accumulates within neurons and competes with tau on microtubules, then plaques on the outside might be less central to the earliest damage than once thought.<\/p>\n\n\n\n<p>The theory also fits with what scientists know about aging. As people get older, the brain\u2019s cellular recycling system, called autophagy, tends to slow down. Under normal conditions, autophagy helps clear proteins like amyloid beta from cells. If that cleanup process weakens, amyloid beta could build up inside neurons, eventually reaching levels high enough to interfere with tau\u2019s role on microtubules.<\/p>\n\n\n\n<p>Other findings from the broader Alzheimer\u2019s field also line up. Some studies have suggested that lithium, a drug long used to treat mood disorders, may lower Alzheimer\u2019s risk. Separate research has shown that lithium can stabilize microtubules. That connection hints that protecting microtubules \u2014 rather than only attacking protein clumps \u2014 might help counteract the disruptive effects of amyloid beta.<\/p>\n\n\n\n<p>If further studies confirm the new model, it could shift how scientists design therapies. Instead of focusing solely on dissolving plaques or tangles, future treatments might aim to keep amyloid beta from binding to microtubules, strengthen tau\u2019s grip on those structures, or boost the cell\u2019s ability to clear excess amyloid beta before it causes trouble.<\/p>\n\n\n\n<p>Julian noted the work offers a way to connect many scattered pieces of Alzheimer\u2019s research into a single, coherent picture. <\/p>\n\n\n\n<p>\u201cThis idea helps make sense of many results that previously seemed unrelated,\u201d he said. \u201cIt gives us a clearer picture of what may be going wrong inside neurons and where new treatments might start.\u201d<\/p>\n\n\n\n<p>For patients and families, any new theory still has to translate into real-world advances, and that will take time. But by shifting attention to the microscopic highways inside brain cells \u2014 and the competition playing out on their surface \u2014 the UC Riverside-led study opens a fresh path toward understanding and, eventually, treating one of the most devastating brain diseases of aging.<\/p>\n\n\n\n<div style=\"height:14px\" aria-hidden=\"true\" class=\"wp-block-spacer\"><\/div>\n\n\n\n<p><strong>Source: <\/strong><a href=\"https:\/\/news.ucr.edu\/articles\/2026\/03\/18\/key-alzheimers-proteins-are-competing-inside-brain-cells\" target=\"_blank\" rel=\"noopener\" title=\"\">University of California, Riverside<\/a><\/p>\n","protected":false},"excerpt":{"rendered":"<p>A UC Riverside-led team has found that two hallmark Alzheimer\u2019s proteins compete for the same spots inside brain cells, potentially derailing neurons from within. The work offers a simple, unifying theory that could redirect how scientists design future therapies.<\/p>\n","protected":false},"author":3,"featured_media":0,"comment_status":"open","ping_status":"open","sticky":false,"template":"single-no-separators","format":"standard","meta":{"_acf_changed":false,"_uag_custom_page_level_css":"","_monsterinsights_skip_tracking":false,"_monsterinsights_sitenote_active":false,"_monsterinsights_sitenote_note":"","_monsterinsights_sitenote_category":0,"footnotes":""},"categories":[12],"tags":[207],"class_list":["post-35180","post","type-post","status-publish","format-standard","hentry","category-health","tag-uc-riverside"],"acf":[],"aioseo_notices":[],"uagb_featured_image_src":{"full":false,"thumbnail":false,"medium":false,"medium_large":false,"large":false,"1536x1536":false,"2048x2048":false},"uagb_author_info":{"display_name":"The University Network","author_link":"https:\/\/www.tun.com\/home\/author\/funky_junkie\/"},"uagb_comment_info":0,"uagb_excerpt":"A UC Riverside-led team has found that two hallmark Alzheimer\u2019s proteins compete for the same spots inside brain cells, potentially derailing neurons from within. The work offers a simple, unifying theory that could redirect how scientists design future therapies.","_links":{"self":[{"href":"https:\/\/www.tun.com\/home\/wp-json\/wp\/v2\/posts\/35180","targetHints":{"allow":["GET"]}}],"collection":[{"href":"https:\/\/www.tun.com\/home\/wp-json\/wp\/v2\/posts"}],"about":[{"href":"https:\/\/www.tun.com\/home\/wp-json\/wp\/v2\/types\/post"}],"author":[{"embeddable":true,"href":"https:\/\/www.tun.com\/home\/wp-json\/wp\/v2\/users\/3"}],"replies":[{"embeddable":true,"href":"https:\/\/www.tun.com\/home\/wp-json\/wp\/v2\/comments?post=35180"}],"version-history":[{"count":8,"href":"https:\/\/www.tun.com\/home\/wp-json\/wp\/v2\/posts\/35180\/revisions"}],"predecessor-version":[{"id":35259,"href":"https:\/\/www.tun.com\/home\/wp-json\/wp\/v2\/posts\/35180\/revisions\/35259"}],"wp:attachment":[{"href":"https:\/\/www.tun.com\/home\/wp-json\/wp\/v2\/media?parent=35180"}],"wp:term":[{"taxonomy":"category","embeddable":true,"href":"https:\/\/www.tun.com\/home\/wp-json\/wp\/v2\/categories?post=35180"},{"taxonomy":"post_tag","embeddable":true,"href":"https:\/\/www.tun.com\/home\/wp-json\/wp\/v2\/tags?post=35180"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}