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DENN domain-containing protein FAM45A regulates the homeostasis of late/multivesicular endosomes

Zhang, Jianjian, Zhang, Kangning, Qi, Lijuan, Hu, Qiuming, Shen, Zhen, Liu, Bowen, Deng, Jiaxin, Zhang, Changsong, Zhang, Yanling·2019·Biochimica et Biophysica Acta (BBA) - Molecular Cell Research
DOI 10.1016/j.bbamcr.2019.02.006
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Abstract

DENN (differentially expressed in normal cells and neoplasia) domain-containing proteins are a family of guanine nucleotide exchange factors (GEFs) for Rab small GTPases and coordinate a plethora of intracellular membrane trafficking events. FAM45A is a non-classical DENN domain protein, whose function was unknown. In this study, we characterized cellular roles of FAM45A. We found that FAM45A localized mainly in late/multivesicular endosomes. Depletion of FAM45A resulted in clustering of endosomes to the perinuclear region. The endocytosis of EGF receptor was impaired in FAM45A knockdown cells due to a delay in the early-to-late endosome transition. Furthermore, the secretion of selected exosome subpopulations was also attenuated in FAM45A knockdown cells. Consistent with these results, Rab27a and Rab27b, two Rabs involved in endosome motility and exosome biogenesis, were found to act downstream of FAM45A pathway. FAM45A colocalized with Rab27a/b and formed complex with them in a nucleotide-dependent manner. Taken together, FAM45A defines a novel regulatory step in the homeostasis of late endocytic pathway, including endosomal positioning, maturation and secretion, possibly through activating Rab proteins such as Rab27a/b.

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  • Recycling events involving Retriever are dependent on proper activation of the WASH complex.

    “Furthermore, recycling events involving Retriever are also dependent on proper activation of the WASH complex, which when dysregulated, prevents the recycling of LDL receptor family members and other Retriever cargoes22,24.”

    From Structural organization of the retriever–CCC endosomal recycling complex (2024) · cites this paper as [24]

  • Retriever and CCC play crucial roles in endosomal recycling of membrane proteins.

    “Retriever, a trimeric complex of VPS35L, VPS26C and VPS29, together with the CCC complex comprising CCDC22, CCDC93, and COMMD proteins, plays a crucial role in this process.”

    From Structural organization of the retriever–CCC endosomal recycling complex (2024) · cites this paper as [24]

  • No putative RAB effector protein(s) have yet been identified, although there is evidence for an association with RAB27.

    “no putative RAB effector protein(s) have yet been identified, although there is evidence for an association with RAB27.69”

    From Structure of the endosomal Commander complex linked to Ritscher-Schinzel syndrome (2023) · cites this paper as [69]

  • DENND10 localizes to late endosomes, and its knockdown perturbs aspects of endosomal morphology and function, although it appears dispensable for assembly of Commander.

    “DENND10 localizes to late endosomes, and its knockdown perturbs aspects of endosomal morphology and function,21,69 although it appears dispensable for assembly of Commander.21”

    From Structure of the endosomal Commander complex linked to Ritscher-Schinzel syndrome (2023) · cites this paper as [69]

  • DENND10 is mainly localized in endosomes and lysosomes, where it regulates the positioning, maturation, and secretion of endosomes.

    “In a previous study, we found that DENND10 is mainly localized in endosomes and lysosomes, where it regulates the positioning, maturation, and secretion of endosomes.24”

    From Endosomal protein DENND10 promotes developmental competence of neurite extension (2025) · cites this paper as [24]

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Metadata

Authors
Zhang, J., Zhang, K., Qi, L., Hu, Q., Shen, Z., Liu, B., Deng, J., Zhang, C., & Zhang, Y.
Venue
Biochimica et Biophysica Acta (BBA) - Molecular Cell Research
Publisher
Elsevier BV
Published
2019-05
Volume
1866
Issue
5
Pages
916-929
ISSN
0167-4889
DOI
10.1016/j.bbamcr.2019.02.006
Cited by
29
References
9
Language
en
Licence
Funders
  • National Natural Science Foundation of China (31401220, 31571465, 31401173)
  • Soochow University
  • Priority Academic Program Development of Jiangsu Higher Education Institutions
  • Natural Science Foundation of Jiangsu (BE2016656, BRA2018171)
  • Changzhou Science and Technology Bureau (CJ20179029, CE20175037)
  • Health Talents Project for Jiangsu, China (ZDRCC2016020)

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