transmedТрансляционная медицинаTranslational Medicine2311-44952410-5155Almazov National Medical Research Centre, Saint Petersburg, Russia10.18705/2311-4495-2026-13-1-42-59KWZYVZtransmed-1110Research ArticleТКАНЕВЫЕ, КЛЕТОЧНЫЕ, ГЕНОМНЫЕ И ПРОТЕОМНЫЕ ТЕХНОЛОГИИCELL, TISSUE, AND GENE THERAPYЭпишаперомно-липидный интерфейс плазматической мембраны как регулятор клеточной стресс-адаптации и терапевтическая мишень при заболеваниях человекаEpichaperome-Lipid Interface of the Plasma Membrane as a Regulator of Cellular Stress Adaptation and a Therapeutic Target in Human Diseaseshttps://orcid.org/0000-0002-8539-2239ШевцовМ. А.ShevtsovMaxim A.

Максим Алексеевич Шевцов -

доктор биологических наук, ведущий научный сотрудник, Тихорецкий пр., д. 4, Санкт-Петербург, 194064.

Maxim A. Shevtsov, DSc in Biological Science, Senior Researcher,

4, Tikhoretsky ave., St. Petersburg, 194064.

shevtsov-max@mail.ruФедеральное государственное бюджетное учреждение науки «Институт цитологии» Российской академии наукРоссияInstitute of Cytology Russian Academy of ScienceRussian Federation2026210520261314259Copyright © Шевцов М.А., 20262026Шевцов М.А.Shevtsov M.A.Данная работа распространяется под лицензией Creative Commons Attribution 4.0.This work is licensed under a Creative Commons Attribution 4.0 License.https://transmed.almazovcentre.ru/jour/article/view/1110

Плазматическая мембрана клетки функционирует не только как структурный барьер, но и как динамическая регуляторная платформа, интегрирующая стрессовые, механические и метаболические сигналы и координирующая внутриклеточные и межклеточные адаптивные реакции. Она обеспечивает пространственную организацию сигнальных комплексов, способствует компартментализации биохимических процессов и формирует условия для быстрой и избирательной перестройки клеточного ответа на изменения микроокружения. В настоящей работе предложена концепция мембранно-ассоциированного эпишаперома, организованного в функциональной связи с липидными микродоменами и формирующего эпишаперомно-липидный интерфейс — структурно и функционально целостную платформу, объединяющую протеостаз, биофизику мембран и адаптивный сигналинг.

Мембранные белки теплового шока HSP70 и HSP90 координируют внутриклеточные сигнальные каскады, выступая платформами для сборки и стабилизации мультибелковых комплексов, включая рецепторы и киназы. Они поддерживают активность сигнальных путей и регулируют межклеточную коммуникацию через экзосомы, внеклеточные везикулы и туннельные нанотрубки. Кроме того, эти белки участвуют в ремоделировании липидной среды, влияя на организацию липидных рафтов и обеспечивая функциональную пластичность мембранных доменов, что способствует адаптации клеток к изменяющимся условиям. В патологических состояниях, включая опухоли, хроническое воспаление и нейродегенеративные заболевания, эпишаперомно-липидный интерфейс формирует патологически адаптивные сигнальные платформы, способствующие клеточной пластичности, лекарственной резистентности, инвазии и кооперативному поведению клеток. Предлагаемая теория мембранно-ассоциированного эпишаперома расширяет традиционное понимание цитоплазматических шаперонных сетей и предоставляет новую концептуальную основу для разработки диагностических маркеров и трансляционных терапевтических стратегий, направленных на селективное разрушение патологических мембранных платформ. Цель работы — обобщить современные данные о молекулярной организации и функциях эпишаперомно-липидного интерфейса и обсудить его значение в патогенезе социально значимых заболеваний человека.

The cellular plasma membrane functions not only as a structural barrier but also as a dynamic regulatory platform, integrating stress, mechanical, and metabolic signals and coordinating intracellular and intercellular adaptive responses. It ensures the spatial organization of signaling complexes, promotes compartmentalization of biochemical processes, and creates conditions for rapid and selective reorganization of the cellular response to microenvironmental changes. This review proposes the concept of a membrane-associated epichaperome, organized in functional association with lipid microdomains and forming an epichaperome-lipid interface — a structurally and functionally integrated platform that unites proteostasis, membrane biophysics, and adaptive signaling.

The membrane heat shock proteins HSP70 and HSP90 coordinate intracellular signaling cascades, serving as platforms for the assembly and stabilization of multiprotein complexes, including receptors and kinases. They support the activity of signaling pathways and regulate intercellular communication via exosomes, extracellular vesicles, and tunneling nanotubes. Furthermore, these proteins participate in the remodeling of the lipid environment, influencing the organization of lipid rafts and ensuring the functional plasticity of membrane domains, which facilitates cellular adaptation to changing conditions. In pathological conditions, including tumors, chronic inflammation, and neurodegenerative diseases, the epichaperome-lipid interface forms pathologically adaptive signaling platforms that promote cellular plasticity, drug resistance, invasion, and cooperative behavior. The proposed theory of the membrane-associated epichaperome expands the traditional understanding of cytoplasmic chaperone networks and provides a new conceptual basis for the development of diagnostic markers and translational therapeutic strategies aimed at the selective disruption of pathological membrane platforms. The aim of the work is to summarize modern data on the molecular organization and functions of the epichaperome-lipid interface and discuss its importance in the pathogenesis of socially significant human diseases.

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The authors declare that there are no conflicts of interest present.