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Transmembrane protein 268 (TMEM268) is a single-pass transmembrane protein of 342 amino acids, with two transmembrane domains and several alternative splice variants. It is most highly expressed in immune cells such as monocytes and macrophages and is upregulated in gastric cancer tissues. TMEM268 functions by interacting with integrin subunits such as ITGB4 (β4) and ITGAM (CD11b), stabilizing their cell surface expression and promoting cell–matrix adhesion, cytoskeletal integrity, and migration of both tumor and immune cells. In cancer, TMEM268 enhances tumor cell adhesion and proliferation, favoring tumorigenesis and metastasis. In immunology, TMEM268 is necessary for efficient phagocyte adhesion, migration, and bacterial clearance, with knockout models showing impaired host defense and worsened sepsis. The molecular mechanisms involve regulation of integrin ubiquitylation and interaction with cytoskeletal scaffolding proteins (PLEC, FLNA). No therapeutic agents targeting TMEM268 have yet been developed or clinically approved.
Not established for drugs. As a drug target, mechanisms would hypothesize disruption or stabilization of integrin-mediated adhesion, cytoskeleton remodeling, or immune cell migration
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