A dileucine motif in TMEM163 is essential for its binding with both AP-3 and BLOC-1 complex.

Zhuang Qi, Yefeng Yuan, Wei Li

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Article in The Journal of biological chemistry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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3 authors.

Zhuang QiLaboratory for Genetics of Birth Defects, Beijing Pediatric Research Institute, MOE Key Laboratory of Major Diseases in Children, Genetics and Birth Defects Control Center, National Center for Children's Health, Beijing Children's Hospital, Capital Medical University, Beijing, China.

Yefeng YuanLaboratory for Genetics of Birth Defects, Beijing Pediatric Research Institute, MOE Key Laboratory of Major Diseases in Children, Genetics and Birth Defects Control Center, National Center for Children's Health, Beijing Children's Hospital, Capital Medical University, Beijing, China. Electronic address: yyfeng6886@sina.cn.

Wei LiLaboratory for Genetics of Birth Defects, Beijing Pediatric Research Institute, MOE Key Laboratory of Major Diseases in Children, Genetics and Birth Defects Control Center, National Center for Children's Health, Beijing Children's Hospital, Capital Medical University, Beijing, China; Henan Key Laboratory of Genetic and Developmental Disorders, Institute of Children's Health, Henan Academy of Medical Sciences, Zhengzhou, China; Zhengzhou Hospital of Beijing Children's Hospital, Zhengzhou, China. Electronic address: liwei@bch.com.cn.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Defects in Hermansky-Pudlak syndrome protein associated complexes impair the biogenesis of lysosome-related organelles (e.g. platelet dense granule). Transmembrane protein 163 (TMEM163), a zinc transporter, is drastically reduced in platelets of AP-3-, BLOC-1-, and BLOC-2-deficient Hermansky-Pudlak syndrome mice and patients, but the mechanistic basis is unclear. We here found that TMEM163 was reduced and degraded primarily via the proteasome in a variety of deficient MEG-01 cells of endosomal trafficking complexes (AP-1, AP-2, AP-3, BLOC-1, BLOC-2). A conserved N-terminal acidic dileucine motif (LEDRGL

Indexed as

Adaptor Protein Complex 3Membrane ProteinsNerve Tissue ProteinsAmino Acid MotifsAnimalsDNA-Binding ProteinsHumansMiceProtein BindingTranscription FactorsAdaptor Protein Complex 3BLOC1S1 protein, humanDNA-Binding Proteinsenhancer-binding protein AP-3Membrane ProteinsNerve Tissue ProteinsTranscription Factorsdileucine motifHermansky-Pudlak syndromeHPACsplatelet dense granulesTMEM163

Identifiers

PMID41985787

DOI10.1016/j.jbc.2026.111451

PMCPMC13195334

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