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Article ; Online: Establishment of a synchronized tyrosinase transport system revealed a role of Tyrp1 in efficient melanogenesis by promoting tyrosinase targeting to melanosomes.

Nakamura, Hikari / Fukuda, Mitsunori

2024 Volume 14, Issue 1, Page(s) 2529

Abstract: Tyrosinase (Tyr) is a key enzyme in the process of melanin synthesis that occurs exclusively within specialized organelles called melanosomes in melanocytes. Tyr is synthesized and post-translationally modified independently of the formation of ... ...

Abstract	Tyrosinase (Tyr) is a key enzyme in the process of melanin synthesis that occurs exclusively within specialized organelles called melanosomes in melanocytes. Tyr is synthesized and post-translationally modified independently of the formation of melanosome precursors and then transported to immature melanosomes by a series of membrane trafficking events that includes endoplasmic reticulum (ER)-to-Golgi transport, post-Golgi trafficking, and endosomal transport. Although several important regulators of Tyr transport have been identified, their precise role in each Tyr transport event is not fully understood, because Tyr is present in several melanocyte organelles under steady-state conditions, thereby precluding the possibility of determining where Tyr is being transported at any given moment. In this study, we established a novel synchronized Tyr transport system in Tyr-knockout B16-F1 cells by using Tyr tagged with an artificial oligomerization domain FM4 (named Tyr-EGFP-FM4). Tyr-EGFP-FM4 was initially trapped at the ER under oligomerized conditions, but at 30 min after chemical dissociation into monomers, it was transported to the Golgi and at 9 h reached immature melanosomes. Melanin was then detected at 12 h after the ER exit of Tyr-EGFP-FM4. By using this synchronized Tyr transport system, we were able to demonstrate that Tyr-related protein 1 (Tyrp1), another melanogenic enzyme, is a positive regulator of efficient Tyr targeting to immature melanosomes. Thus, the synchronized Tyr transport system should serve as a useful tool for analyzing the molecular mechanism of each Tyr transport event in melanocytes as well as in the search for new drugs or cosmetics that artificially regulate Tyr transport.
MeSH term(s)	Melanosomes/metabolism ; Monophenol Monooxygenase/metabolism ; Melanins/metabolism ; Melanogenesis ; Melanocytes/metabolism
Chemical Substances	Monophenol Monooxygenase (EC 1.14.18.1) ; Melanins
Language	English
Publishing date	2024-01-30
Publishing country	England
Document type	Journal Article
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/s41598-024-53072-6
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Article ; Online: Rab GTPases: Key players in melanosome biogenesis, transport, and transfer.

Fukuda, Mitsunori

Pigment cell & melanoma research

2020 Volume 34, Issue 2, Page(s) 222–235

Abstract: Melanosomes are specialized intracellular organelles that produce and store melanin pigments in melanocytes, which are present in several mammalian tissues and organs, including the skin, hair, and eyes. Melanosomes form and mature stepwise (stages I-IV) ...

Abstract	Melanosomes are specialized intracellular organelles that produce and store melanin pigments in melanocytes, which are present in several mammalian tissues and organs, including the skin, hair, and eyes. Melanosomes form and mature stepwise (stages I-IV) in melanocytes and then are transported toward the plasma membrane along the cytoskeleton. They are subsequently transferred to neighboring keratinocytes by a largely unknown mechanism, and incorporated melanosomes are transported to the perinuclear region of the keratinocytes where they form melanin caps. Melanocytes also extend several dendrites that facilitate the efficient transfer of the melanosomes to the keratinocytes. Since the melanosome biogenesis, transport, and transfer steps require multiple membrane trafficking processes, Rab GTPases that are conserved key regulators of membrane traffic in all eukaryotes are crucial for skin and hair pigmentation. Dysfunctions of two Rab isoforms, Rab27A and Rab38, are known to cause a hypopigmentation phenotype in human type 2 Griscelli syndrome patients and in chocolate mice (related to Hermansky-Pudlak syndrome), respectively. In this review article, I review the literature on the functions of each Rab isoform and its upstream and downstream regulators in mammalian melanocytes and keratinocytes.
MeSH term(s)	Animals ; Humans ; Melanins/metabolism ; Melanocytes/cytology ; Melanocytes/metabolism ; Melanosomes/metabolism ; Protein Transport ; rab GTP-Binding Proteins/genetics ; rab GTP-Binding Proteins/metabolism
Chemical Substances	Melanins ; rab GTP-Binding Proteins (EC 3.6.5.2)
Language	English
Publishing date	2020-10-14
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2409570-9
ISSN	1755-148X ; 1600-0749 ; 0893-5785 ; 1755-1471
ISSN (online)	1755-148X ; 1600-0749
ISSN	0893-5785 ; 1755-1471
DOI	10.1111/pcmr.12931
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Zs.A 2444: Show issues

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Article ; Online: Large Rab GTPase Rab44 regulates microtubule-dependent retrograde melanosome transport in melanocytes.

Maruta, Yuto / Fukuda, Mitsunori

The Journal of biological chemistry

2022 Volume 298, Issue 11, Page(s) 102508

Abstract: Melanosomes are melanin-containing organelles in melanocytes, and they are responsible for skin and hair pigmentation in mammals. The intracellular distribution of melanosomes is mainly determined by the balance between their anterograde transport on ... ...

Abstract	Melanosomes are melanin-containing organelles in melanocytes, and they are responsible for skin and hair pigmentation in mammals. The intracellular distribution of melanosomes is mainly determined by the balance between their anterograde transport on actin filaments and retrograde transport on microtubules. Although we have shown previously that melanoregulin and Rab36 serve as cargo receptors on melanosomes for retrograde transport, their knockdown does not completely inhibit retrograde melanosome transport, suggesting the existence of an additional cargo receptor(s) in melanocytes. In this study, we investigated the possible involvement of an atypical large Rab, Rab44, which also contains EF-hand domains and a coiled-coil domain, in retrograde melanosome transport in mouse melanocytes (Rab27A-deficient melan-ash cells). Our results showed that Rab44 localizes on mature melanosomes through lipidation of its C-terminal Rab-like GTPase domain, and that its knockdown results in suppression of retrograde melanosome transport. In addition, our biochemical analysis indicated that Rab44 interacts with the dynein-dynactin motor complex via its coiled-coil domain-containing middle region. Since simultaneous depletion of Rab44, melanoregulin, and Rab36 resulted in almost complete inhibition of retrograde melanosome transport, we propose that Rab44 is the third cargo receptor. We also showed that the N-terminal region of Rab44, which contains EF-hand domains, is required for both retrograde melanosome transport and its Ca
MeSH term(s)	Mice ; Animals ; Melanosomes/metabolism ; rab GTP-Binding Proteins/genetics ; rab GTP-Binding Proteins/metabolism ; Melanocytes/metabolism ; Biological Transport/physiology ; Microtubules/metabolism ; Dynactin Complex/metabolism ; Mammals/metabolism ; Adaptor Proteins, Vesicular Transport/metabolism
Chemical Substances	rab GTP-Binding Proteins (EC 3.6.5.2) ; Dynactin Complex ; melanoregulin protein, mouse ; Adaptor Proteins, Vesicular Transport
Language	English
Publishing date	2022-09-17
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1016/j.jbc.2022.102508
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Article ; Online: Vps9d1 regulates tubular endosome formation through specific activation of Rab22A.

Nakashima, Shumpei / Matsui, Takahide / Fukuda, Mitsunori

Journal of cell science

2023 Volume 136, Issue 6

Abstract: The small GTPase Rab22A is an important regulator of the formation of tubular endosomes, which are one of the types of recycling endosome compartments of the clathrin-independent endocytosis pathway. In order to regulate tubular endosome formation, ... ...

Abstract	The small GTPase Rab22A is an important regulator of the formation of tubular endosomes, which are one of the types of recycling endosome compartments of the clathrin-independent endocytosis pathway. In order to regulate tubular endosome formation, Rab22A must be activated by a specific guanine-nucleotide-exchange factor (GEF); however, all of the GEFs that have been reported to exhibit Rab22A-GEF activity in vitro also activate Rab5A, an essential regulator of the clathrin-mediated endocytosis pathway, and no Rab22A-specific GEF has ever been identified. Here, we identified Vps9d1, a previously uncharacterized vacuolar protein sorting 9 (VPS9) domain-containing protein, as a novel Rab22A-GEF. The formation of tubular endosome structures was found to be severely impaired in Vps9d1-depleted HeLa cells, but Rab5A localization was unaffected. Expression of a constitutively active Rab22A mutant in Vps9d1-depleted HeLa cells restored tubular endosomes, but expression of a GEF-activity-deficient Vps9d1 mutant did not. Moreover, Vps9d1 depletion altered the distribution of clathrin-independent endocytosed cargos and impaired their recycling. Our findings indicate that Vps9d1 promotes tubular endosome formation by specifically activating Rab22A.
MeSH term(s)	Humans ; HeLa Cells ; rab GTP-Binding Proteins/genetics ; rab GTP-Binding Proteins/metabolism ; Endosomes/metabolism ; Endocytosis/physiology ; Protein Transport/physiology ; Clathrin/metabolism ; Guanine Nucleotide Exchange Factors/genetics ; Guanine Nucleotide Exchange Factors/metabolism
Chemical Substances	rab GTP-Binding Proteins (EC 3.6.5.2) ; Clathrin ; Guanine Nucleotide Exchange Factors ; RAB22A protein, human
Language	English
Publishing date	2023-03-08
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2993-2
ISSN	1477-9137 ; 0021-9533
ISSN (online)	1477-9137
ISSN	0021-9533
DOI	10.1242/jcs.260522
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Zs.A 1200: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (1.OG) ab Jg. 2022: Lesesaal (EG)
Zs.MG 14: Show issues

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Article ; Online: VAMP5 and distinct sets of cognate Q-SNAREs mediate exosome release.

Matsui, Takahide / Sakamaki, Yuriko / Hiragi, Shu / Fukuda, Mitsunori

Cell structure and function

2023 Volume 48, Issue 2, Page(s) 187–198

Abstract: Small extracellular vesicles (sEVs) are largely classified into two types, plasma-membrane derived sEVs and endomembrane-derived sEVs. The latter type (referred to as exosomes herein) is originated from late endosomes or multivesicular bodies (MVBs). In ... ...

Abstract	Small extracellular vesicles (sEVs) are largely classified into two types, plasma-membrane derived sEVs and endomembrane-derived sEVs. The latter type (referred to as exosomes herein) is originated from late endosomes or multivesicular bodies (MVBs). In order to release exosomes extracellularly, MVBs must fuse with the plasma membrane, not with lysosomes. In contrast to the mechanism responsible for MVB-lysosome fusion, the mechanism underlying the MVB-plasma membrane fusion is poorly understood. Here, we systematically analyze soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) family proteins and identify VAMP5 as an MVB-localized SNARE protein required for exosome release. Depletion of VAMP5 in HeLa cells impairs exosome release. Mechanistically, VAMP5 mediates exosome release by interacting with SNAP47 and plasma membrane SNARE Syntaxin 1 (STX1) or STX4 to release exosomes. VAMP5 is also found to mediate asymmetric exosome release from polarized Madin-Darby canine kidney (MDCK) epithelial cells through interaction with the distinct sets of Q-SNAREs, suggesting that VAMP5 is a general exosome regulator in both polarized cells and non-polarized cells.Key words: exosome, small extracellular vesicle (sEV), multivesicular body, SNARE, VAMP5.
MeSH term(s)	Humans ; Animals ; Dogs ; Exosomes/metabolism ; HeLa Cells ; Cell Membrane/metabolism ; SNARE Proteins/metabolism ; Qa-SNARE Proteins/metabolism
Chemical Substances	SNARE Proteins ; Qa-SNARE Proteins
Language	English
Publishing date	2023-09-14
Publishing country	Japan
Document type	Journal Article
ZDB-ID	197293-5
ISSN	1347-3700 ; 0386-7196
ISSN (online)	1347-3700
ISSN	0386-7196
DOI	10.1247/csf.23067
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Zs.A 1294: Show issues

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Article ; Online: Knockout analysis of Rab6 effector proteins revealed the role of VPS52 in the secretory pathway.

Homma, Yuta / Fukuda, Mitsunori

Biochemical and biophysical research communications

2021 Volume 561, Page(s) 151–157

Abstract: Rab small GTPases regulate intracellular membrane trafficking by interacting with specific binding proteins called Rab effectors. Although Rab6 is implicated in basement membrane formation and secretory cargo trafficking, its precise regulatory ... ...

Abstract	Rab small GTPases regulate intracellular membrane trafficking by interacting with specific binding proteins called Rab effectors. Although Rab6 is implicated in basement membrane formation and secretory cargo trafficking, its precise regulatory mechanisms have remained largely unknown. In the present study we established five knockout cell lines for candidate Rab6 effectors and discovered that knockout of VPS52, a subunit of the GARP complex, resulted in attenuated secretion and lysosomal accumulation of secretory cargos, the same as Rab6-knockout does. We also evaluated the functional importance of the previously uncharacterized C-terminal region of VPS52 for restoring these phenotypes, as well as for the sorting of lysosomal proteins. Our findings suggest that VPS52 is an effector protein that is responsible for the Rab6-dependent secretory cargo trafficking.
MeSH term(s)	Animals ; CRISPR-Cas Systems ; Cells, Cultured ; Dogs ; Gene Knockdown Techniques/methods ; Golgi Apparatus ; Humans ; Intracellular Membranes ; Lysosomes/metabolism ; Protein Transport ; Secretory Pathway/physiology ; Vesicular Transport Proteins/antagonists & inhibitors ; Vesicular Transport Proteins/genetics ; Vesicular Transport Proteins/metabolism ; rab GTP-Binding Proteins/metabolism
Chemical Substances	Rab6 protein ; VPS52 protein, human ; Vesicular Transport Proteins ; rab GTP-Binding Proteins (EC 3.6.5.2)
Language	English
Publishing date	2021-05-21
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	205723-2
ISSN	1090-2104 ; 0006-291X ; 0006-291X
ISSN (online)	1090-2104 ; 0006-291X
ISSN	0006-291X
DOI	10.1016/j.bbrc.2021.05.009
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Zs.A 116: Show issues

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Article ; Online: Multiple Roles of VARP in Endosomal Trafficking: Rabs, Retromer Components and R-SNARE VAMP7 Meet on VARP.

Fukuda, Mitsunori

Traffic (Copenhagen, Denmark)

2016 Volume 17, Issue 7, Page(s) 709–719

Abstract: VARP (VPS9-ankyrin-repeat protein, also known as ANKRD27) was originally identified as an N-terminal VPS9 (vacuolar protein sorting 9)-domain-containing protein that possesses guanine nucleotide exchange factor (GEF) activity toward small GTPase Rab21 ... ...

Abstract	VARP (VPS9-ankyrin-repeat protein, also known as ANKRD27) was originally identified as an N-terminal VPS9 (vacuolar protein sorting 9)-domain-containing protein that possesses guanine nucleotide exchange factor (GEF) activity toward small GTPase Rab21 and contains two ankyrin repeat (ANKR) domains in its central region. A number of VARP-interacting molecules have been identified during the past five years, and considerable attention is now being directed to the multiple roles of VARP in endosomal trafficking. More specifically, VARP is now known to interact with three different types of key membrane trafficking regulators, i.e. small GTPase Rabs (Rab32, Rab38 and Rab40C), the retromer complex (a sorting nexin dimer, VPS26, VPS29 and VPS35) and R-SNARE VAMP7. By binding to several of these molecules, VARP regulates endosomal trafficking, which underlies a variety of cellular events, including melanogenic enzyme trafficking to melanosomes, dendrite outgrowth of melanocytes, neurite outgrowth and retromer-mediated endosome-to-plasma membrane sorting of transmembrane proteins.
MeSH term(s)	Animals ; Dendrites/metabolism ; Endosomes/metabolism ; Guanine Nucleotide Exchange Factors/chemistry ; Guanine Nucleotide Exchange Factors/genetics ; Guanine Nucleotide Exchange Factors/metabolism ; Humans ; Intracellular Membranes/metabolism ; Ligands ; Melanocytes/metabolism ; Melanosomes/metabolism ; Membrane Proteins/metabolism ; Neuronal Outgrowth/physiology ; Organ Specificity ; Protein Binding ; Protein Transport ; R-SNARE Proteins/chemistry ; R-SNARE Proteins/genetics ; R-SNARE Proteins/metabolism ; rab GTP-Binding Proteins/chemistry ; rab GTP-Binding Proteins/genetics ; rab GTP-Binding Proteins/metabolism
Chemical Substances	ANKRD27 protein, human ; Guanine Nucleotide Exchange Factors ; Ligands ; Membrane Proteins ; R-SNARE Proteins ; VAMP7 protein, human ; rab GTP-Binding Proteins (EC 3.6.5.2)
Language	English
Publishing date	2016-05-13
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	1483852-7
ISSN	1600-0854 ; 1398-9219
ISSN (online)	1600-0854
ISSN	1398-9219
DOI	10.1111/tra.12406
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Zs.A 5634: Show issues

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Article ; Online: The Underlying Rab Network of MRGPRX2-Stimulated Secretion Unveils the Impact of Receptor Trafficking on Secretory Granule Biogenesis and Secretion.

Lazki-Hagenbach, Pia / Kleeblatt, Elisabeth / Fukuda, Mitsunori / Ali, Hydar / Sagi-Eisenberg, Ronit

Cells

2024 Volume 13, Issue 1

Abstract: MRGPRX2, the human member of the MAS-related G-protein-coupled receptors (GPCRs), mediates the immunoglobulin E (IgE)-independent responses of a subset of mast cells (MCs) that are associated with itch, pain, neurogenic inflammation, and pseudoallergy to ...

Abstract	MRGPRX2, the human member of the MAS-related G-protein-coupled receptors (GPCRs), mediates the immunoglobulin E (IgE)-independent responses of a subset of mast cells (MCs) that are associated with itch, pain, neurogenic inflammation, and pseudoallergy to drugs. The mechanisms underlying the responses of MRGPRX2 to its multiple and diverse ligands are still not completely understood. Given the close association between GPCR location and function, and the key role played by Rab GTPases in controlling discrete steps along vesicular trafficking, we aimed to reveal the vesicular pathways that directly impact MRGPRX2-mediated exocytosis by identifying the Rabs that influence this process. For this purpose, we screened 43 Rabs for their functional and phenotypic impacts on MC degranulation in response to the synthetic MRGPRX2 ligand compound 48/80 (c48/80), which is often used as the gold standard of MRGPRX2 ligands, or to substance P (SP), an important trigger of neuroinflammatory MC responses. Results of this study highlight the important roles played by macropinocytosis and autophagy in controlling MRGPRX2-mediated exocytosis, demonstrating a close feedback control between the internalization and post-endocytic trafficking of MRGPRX2 and its triggered exocytosis.
MeSH term(s)	Humans ; Bodily Secretions ; Exocytosis ; Autophagy ; Immunoglobulin E ; Inflammation ; Secretory Vesicles ; Nerve Tissue Proteins ; Receptors, Neuropeptide ; Receptors, G-Protein-Coupled
Chemical Substances	Immunoglobulin E (37341-29-0) ; MRGPRX2 protein, human ; Nerve Tissue Proteins ; Receptors, Neuropeptide ; Receptors, G-Protein-Coupled
Language	English
Publishing date	2024-01-01
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2661518-6
ISSN	2073-4409 ; 2073-4409
ISSN (online)	2073-4409
ISSN	2073-4409
DOI	10.3390/cells13010093
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Article: Knockout analysis of Rab6 effector proteins revealed the role of VPS52 in the secretory pathway

Homma, Yuta / Fukuda, Mitsunori

Biochemical and biophysical research communications. 2021 July 05, v. 561

2021

Abstract	Rab small GTPases regulate intracellular membrane trafficking by interacting with specific binding proteins called Rab effectors. Although Rab6 is implicated in basement membrane formation and secretory cargo trafficking, its precise regulatory mechanisms have remained largely unknown. In the present study we established five knockout cell lines for candidate Rab6 effectors and discovered that knockout of VPS52, a subunit of the GARP complex, resulted in attenuated secretion and lysosomal accumulation of secretory cargos, the same as Rab6-knockout does. We also evaluated the functional importance of the previously uncharacterized C-terminal region of VPS52 for restoring these phenotypes, as well as for the sorting of lysosomal proteins. Our findings suggest that VPS52 is an effector protein that is responsible for the Rab6-dependent secretory cargo trafficking.
Keywords	basement membrane ; guanosinetriphosphatase ; research ; secretion
Language	English
Dates of publication	2021-0705
Size	p. 151-157.
Publishing place	Elsevier Inc.
Document type	Article
Note	NAL-AP-2-clean
ZDB-ID	205723-2
ISSN	0006-291X ; 0006-291X
ISSN (online)	0006-291X
ISSN	0006-291X
DOI	10.1016/j.bbrc.2021.05.009
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Article ; Online: Rab39 and its effector UACA regulate basolateral exosome release from polarized epithelial cells.

Matsui, Takahide / Sakamaki, Yuriko / Nakashima, Shumpei / Fukuda, Mitsunori

Cell reports

2022 Volume 39, Issue 9, Page(s) 110875

Abstract: Exosomes are small extracellular vesicles that originate from the intraluminal vesicles of multivesicular bodies (MVBs). We previously reported that polarized Madin-Darby canine kidney (MDCK) epithelial cells secrete two types of exosomes, apical and ... ...

Abstract	Exosomes are small extracellular vesicles that originate from the intraluminal vesicles of multivesicular bodies (MVBs). We previously reported that polarized Madin-Darby canine kidney (MDCK) epithelial cells secrete two types of exosomes, apical and basolateral exosomes, from different MVBs. However, how these MVBs are selectively targeted to the apical or basolateral membrane remained unknown. Here, we analyze members of the Rab family small GTPases and show that different sets of Rabs mediate asymmetrical exosome release. Rab27, the best-known regulator of MVB transport for exosome release, is specifically but partially involved in apical exosome release, and Rab37, a close homolog of Rab27, is an additional apical exosome regulator. By contrast, Rab39 functions as a specific regulator of basolateral exosome release. Mechanistically, Rab39 interacts with its effector UACA, and UACA then recruits Lyspersin, a component of BLOC-1-related complex (BORC). Our findings suggest that the Rab39-UACA-BORC complex specifically mediates basolateral exosome release.
MeSH term(s)	Animals ; Cell Membrane/metabolism ; Dogs ; Exosomes/metabolism ; Madin Darby Canine Kidney Cells ; Multivesicular Bodies/metabolism ; rab GTP-Binding Proteins/metabolism
Chemical Substances	rab GTP-Binding Proteins (EC 3.6.5.2)
Language	English
Publishing date	2022-06-01
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2649101-1
ISSN	2211-1247 ; 2211-1247
ISSN (online)	2211-1247
ISSN	2211-1247
DOI	10.1016/j.celrep.2022.110875
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