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Article ; Online: The oncogene cyclin D1 promotes bipolar spindle integrity under compressive force.

Sutanto, Renaldo / Neahring, Lila / Serra Marques, Andrea / Jacobo Jacobo, Mauricio / Kilinc, Seda / Goga, Andrei / Dumont, Sophie

PloS one

2024 Volume 19, Issue 3, Page(s) e0296779

Abstract: The mitotic spindle is the bipolar, microtubule-based structure that segregates chromosomes at each cell division. Aberrant spindles are frequently observed in cancer cells, but how oncogenic transformation affects spindle mechanics and function, ... ...

Abstract	The mitotic spindle is the bipolar, microtubule-based structure that segregates chromosomes at each cell division. Aberrant spindles are frequently observed in cancer cells, but how oncogenic transformation affects spindle mechanics and function, particularly in the mechanical context of solid tumors, remains poorly understood. Here, we constitutively overexpress the oncogene cyclin D1 in human MCF10A cells to probe its effects on spindle architecture and response to compressive force. We find that cyclin D1 overexpression increases the incidence of spindles with extra poles, centrioles, and chromosomes. However, it also protects spindle poles from fracturing under compressive force, a deleterious outcome linked to multipolar cell divisions. Our findings suggest that cyclin D1 overexpression may adapt cells to increased compressive stress, possibly contributing to its prevalence in cancers such as breast cancer by allowing continued proliferation in mechanically challenging environments.
MeSH term(s)	Humans ; Centrioles ; Centrosome ; Cyclin D1/genetics ; Mitosis ; Oncogenes ; Spindle Apparatus/genetics
Chemical Substances	Cyclin D1 (136601-57-5) ; CCND1 protein, human
Language	English
Publishing date	2024-03-13
Publishing country	United States
Document type	Journal Article
ZDB-ID	2267670-3
ISSN	1932-6203 ; 1932-6203
ISSN (online)	1932-6203
ISSN	1932-6203
DOI	10.1371/journal.pone.0296779
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Article ; Online: Shining light on spindle positioning.

Serra-Marques, Andrea / Dumont, Sophie

eLife

2018 Volume 7

Abstract: Optogenetic approaches are leading to a better understanding of the forces that determine the plane of cell division. ...

Abstract	Optogenetic approaches are leading to a better understanding of the forces that determine the plane of cell division.
MeSH term(s)	Cell Division ; Dynactin Complex ; Dyneins ; Microtubules ; Spindle Apparatus
Chemical Substances	Dynactin Complex ; Dyneins (EC 3.6.4.2)
Language	English
Publishing date	2018-07-09
Publishing country	England
Document type	Journal Article ; Comment
ZDB-ID	2687154-3
ISSN	2050-084X ; 2050-084X
ISSN (online)	2050-084X
ISSN	2050-084X
DOI	10.7554/eLife.38748
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Article ; Online: The mitotic protein NuMA plays a spindle-independent role in nuclear formation and mechanics.

Serra-Marques, Andrea / Houtekamer, Ronja / Hintzen, Dorine / Canty, John T / Yildiz, Ahmet / Dumont, Sophie

The Journal of cell biology

2020 Volume 219, Issue 12

Abstract: Eukaryotic cells typically form a single, round nucleus after mitosis, and failures to do so can compromise genomic integrity. How mammalian cells form such a nucleus remains incompletely understood. NuMA is a spindle protein whose disruption results in ... ...

Abstract	Eukaryotic cells typically form a single, round nucleus after mitosis, and failures to do so can compromise genomic integrity. How mammalian cells form such a nucleus remains incompletely understood. NuMA is a spindle protein whose disruption results in nuclear fragmentation. What role NuMA plays in nuclear integrity, and whether its perceived role stems from its spindle function, are unclear. Here, we use live imaging to demonstrate that NuMA plays a spindle-independent role in forming a single, round nucleus. NuMA keeps the decondensing chromosome mass compact at mitotic exit and promotes a mechanically robust nucleus. NuMA's C terminus binds DNA in vitro and chromosomes in interphase, while its coiled-coil acts as a central regulatory and structural element: it prevents NuMA from binding chromosomes at mitosis, regulates its nuclear mobility, and is essential for nuclear formation. Thus, NuMA plays a structural role over the cell cycle, building and maintaining the spindle and nucleus, two of the cell's largest structures.
MeSH term(s)	Cell Cycle Proteins/genetics ; Cell Cycle Proteins/metabolism ; Cell Nucleus/genetics ; Cell Nucleus/metabolism ; Chromosomes, Human/genetics ; Chromosomes, Human/metabolism ; DNA/genetics ; DNA/metabolism ; HEK293 Cells ; Humans ; Interphase ; Mitosis ; Spindle Apparatus/genetics ; Spindle Apparatus/metabolism
Chemical Substances	Cell Cycle Proteins ; NUMA1 protein, human ; DNA (9007-49-2)
Language	English
Publishing date	2020-10-09
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	218154-x
ISSN	1540-8140 ; 0021-9525
ISSN (online)	1540-8140
ISSN	0021-9525
DOI	10.1083/jcb.202004202
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Article ; Online: Angiomotin isoform 2 promotes binding of PALS1 to KIF13B at primary cilia and regulates ciliary length and signaling.

Morthorst, Stine Kjær / Nielsen, Camilla / Farinelli, Pietro / Anvarian, Zeinab / Rasmussen, Christina Birgitte R / Serra-Marques, Andrea / Grigoriev, Ilya / Altelaar, Maarten / Fürstenberg, Nicoline / Ludwig, Alexander / Akhmanova, Anna / Christensen, Søren Tvorup / Pedersen, Lotte Bang

Journal of cell science

2022 Volume 135, Issue 12

Abstract: The kinesin-3 motor KIF13B functions in endocytosis, vesicle transport and regulation of ciliary length and signaling. Direct binding of the membrane-associated guanylate kinase (MAGUK) DLG1 to the MAGUK-binding stalk domain of KIF13B relieves motor ... ...

Abstract	The kinesin-3 motor KIF13B functions in endocytosis, vesicle transport and regulation of ciliary length and signaling. Direct binding of the membrane-associated guanylate kinase (MAGUK) DLG1 to the MAGUK-binding stalk domain of KIF13B relieves motor autoinhibition and promotes microtubule plus-end-directed cargo transport. Here, we characterize angiomotin (AMOT) isoform 2 (p80, referred to as Ap80) as a novel KIF13B interactor that promotes binding of another MAGUK, the polarity protein and Crumbs complex component PALS1, to KIF13B. Live-cell imaging analysis indicated that Ap80 is concentrated at and recruits PALS1 to the base of the primary cilium, but is not a cargo of KIF13B itself. Consistent with a ciliary function for Ap80, its depletion led to elongated primary cilia and reduced agonist-induced ciliary accumulation of SMO, a key component of the Hedgehog signaling pathway, whereas Ap80 overexpression caused ciliary shortening. Our results suggest that Ap80 activates KIF13B cargo binding at the base of the primary cilium to regulate ciliary length, composition and signaling.
MeSH term(s)	Angiomotins ; Cilia/metabolism ; Guanylate Kinases ; Hedgehog Proteins/metabolism ; Membrane Proteins/metabolism ; Protein Isoforms
Chemical Substances	Angiomotins ; Hedgehog Proteins ; Membrane Proteins ; Protein Isoforms ; Guanylate Kinases (EC 2.7.4.8)
Language	English
Publishing date	2022-06-24
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.259471
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Article ; Online: Concerted action of kinesins KIF5B and KIF13B promotes efficient secretory vesicle transport to microtubule plus ends.

Serra-Marques, Andrea / Martin, Maud / Katrukha, Eugene A / Grigoriev, Ilya / Peeters, Cathelijn Ae / Liu, Qingyang / Hooikaas, Peter Jan / Yao, Yao / Solianova, Veronika / Smal, Ihor / Pedersen, Lotte B / Meijering, Erik / Kapitein, Lukas C / Akhmanova, Anna

eLife

2020 Volume 9

Abstract: Intracellular transport relies on multiple kinesins, but it is poorly understood which kinesins are present on particular cargos, what their contributions are and whether they act simultaneously on the same cargo. Here, we show that Rab6-positive ... ...

Abstract	Intracellular transport relies on multiple kinesins, but it is poorly understood which kinesins are present on particular cargos, what their contributions are and whether they act simultaneously on the same cargo. Here, we show that Rab6-positive secretory vesicles are transported from the Golgi apparatus to the cell periphery by kinesin-1 KIF5B and kinesin-3 KIF13B, which determine the location of secretion events. KIF5B plays a dominant role, whereas KIF13B helps Rab6 vesicles to reach freshly polymerized microtubule ends, to which KIF5B binds poorly, likely because its cofactors, MAP7-family proteins, are slow in populating these ends. Sub-pixel localization demonstrated that during microtubule plus-end directed transport, both kinesins localize to the vesicle front and can be engaged on the same vesicle. When vesicles reverse direction, KIF13B relocates to the middle of the vesicle, while KIF5B shifts to the back, suggesting that KIF5B but not KIF13B undergoes a tug-of-war with a minus-end directed motor.
MeSH term(s)	HeLa Cells ; Humans ; Kinesins/genetics ; Kinesins/metabolism ; Microtubules ; Protein Transport ; Transport Vesicles ; rab GTP-Binding Proteins/genetics ; rab GTP-Binding Proteins/metabolism
Chemical Substances	KIF5B protein, human ; Rab6 protein ; KIF13B protein, human (EC 3.6.1.-) ; Kinesins (EC 3.6.4.4) ; rab GTP-Binding Proteins (EC 3.6.5.2)
Language	English
Publishing date	2020-11-11
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2687154-3
ISSN	2050-084X ; 2050-084X
ISSN (online)	2050-084X
ISSN	2050-084X
DOI	10.7554/eLife.61302
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Article ; Online: KIF13B establishes a CAV1-enriched microdomain at the ciliary transition zone to promote Sonic hedgehog signalling.

Schou, Kenneth B / Mogensen, Johanne B / Morthorst, Stine K / Nielsen, Brian S / Aleliunaite, Aiste / Serra-Marques, Andrea / Fürstenberg, Nicoline / Saunier, Sophie / Bizet, Albane A / Veland, Iben R / Akhmanova, Anna / Christensen, Søren T / Pedersen, Lotte B

Nature communications

2017 Volume 8, Page(s) 14177

Abstract: Ciliary membrane composition is controlled by transition zone (TZ) proteins such as RPGRIP1, RPGRIPL and NPHP4, which are vital for balanced coordination of diverse signalling systems like the Sonic hedgehog (Shh) pathway. Activation of this pathway ... ...

Abstract	Ciliary membrane composition is controlled by transition zone (TZ) proteins such as RPGRIP1, RPGRIPL and NPHP4, which are vital for balanced coordination of diverse signalling systems like the Sonic hedgehog (Shh) pathway. Activation of this pathway involves Shh-induced ciliary accumulation of Smoothened (SMO), which is disrupted by disease-causing mutations in TZ components. Here we identify kinesin-3 motor protein KIF13B as a novel member of the RPGRIP1N-C2 domain-containing protein family and show that KIF13B regulates TZ membrane composition and ciliary SMO accumulation. KIF13B is upregulated during ciliogenesis and is recruited to the ciliary base by NPHP4, which binds to two distinct sites in the KIF13B tail region, including an RPGRIP1N-C2 domain. KIF13B and NPHP4 are both essential for establishment of a CAV1 membrane microdomain at the TZ, which in turn is required for Shh-induced ciliary SMO accumulation. Thus KIF13B is a novel regulator of ciliary TZ configuration, membrane composition and Shh signalling.
MeSH term(s)	Animals ; Caveolin 1/metabolism ; Cell Line ; Cell Membrane/metabolism ; Cell Membrane/physiology ; Cilia/physiology ; Computational Biology ; Gene Expression Profiling ; Gene Expression Regulation/physiology ; Gene Knockout Techniques ; HEK293 Cells ; Hedgehog Proteins/metabolism ; Humans ; Kinesin/genetics ; Kinesin/metabolism ; Membrane Proteins/genetics ; Membrane Proteins/metabolism ; Mice ; NIH 3T3 Cells ; Protein Domains/physiology ; Proteins/metabolism ; Signal Transduction/physiology ; Smoothened Receptor/metabolism ; Up-Regulation ; Zinc Finger Protein GLI1/genetics ; Zinc Finger Protein GLI1/metabolism
Chemical Substances	CAV1 protein, human ; Caveolin 1 ; GLI1 protein, human ; Hedgehog Proteins ; Membrane Proteins ; NPHP4 protein, human ; NPHP4 protein, mouse ; Proteins ; SHH protein, human ; SMO protein, human ; Smoothened Receptor ; Zinc Finger Protein GLI1 ; KIF13B protein, human (EC 3.6.1.-) ; KIF13b protein, mouse (EC 3.6.1.-) ; Kinesin (EC 3.6.4.4)
Language	English
Publishing date	2017-01-30
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	2041-1723
ISSN (online)	2041-1723
DOI	10.1038/ncomms14177
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Article ; Online: MICAL3 Flavoprotein Monooxygenase Forms a Complex with Centralspindlin and Regulates Cytokinesis.

Liu, Qingyang / Liu, Fan / Yu, Ka Lou / Tas, Roderick / Grigoriev, Ilya / Remmelzwaal, Sanne / Serra-Marques, Andrea / Kapitein, Lukas C / Heck, Albert J R / Akhmanova, Anna

The Journal of biological chemistry

2016 Volume 291, Issue 39, Page(s) 20617–20629

Abstract: During cytokinesis, the antiparallel array of microtubules forming the central spindle organizes the midbody, a structure that anchors the ingressed cleavage furrow and guides the assembly of abscission machinery. Here, we identified a role for the ... ...

Abstract	During cytokinesis, the antiparallel array of microtubules forming the central spindle organizes the midbody, a structure that anchors the ingressed cleavage furrow and guides the assembly of abscission machinery. Here, we identified a role for the flavoprotein monooxygenase MICAL3, an actin disassembly factor, in organizing midbody-associated protein complexes. By combining cell biological assays with cross-linking mass spectrometry, we show that MICAL3 is recruited to the central spindle and the midbody through a direct interaction with the centralspindlin component MKLP1. Knock-out of MICAL3 leads to an increased frequency of cytokinetic failure and a delayed abscission. In a mechanism independent of its enzymatic activity, MICAL3 targets the adaptor protein ELKS and Rab8A-positive vesicles to the midbody, and the depletion of ELKS and Rab8A also leads to cytokinesis defects. We propose that MICAL3 acts as a midbody-associated scaffold for vesicle targeting, which promotes maturation of the intercellular bridge and abscission.
MeSH term(s)	Adaptor Proteins, Signal Transducing/genetics ; Adaptor Proteins, Signal Transducing/metabolism ; Cell Cycle Proteins/genetics ; Cell Cycle Proteins/metabolism ; Cytokinesis/physiology ; Gene Knockdown Techniques ; HeLa Cells ; Humans ; Microtubule-Associated Proteins/genetics ; Microtubule-Associated Proteins/metabolism ; Mixed Function Oxygenases/genetics ; Mixed Function Oxygenases/metabolism ; Nerve Tissue Proteins/genetics ; Nerve Tissue Proteins/metabolism ; Phosphoproteins/genetics ; Phosphoproteins/metabolism ; Spindle Apparatus/genetics ; Spindle Apparatus/metabolism ; rab GTP-Binding Proteins/genetics ; rab GTP-Binding Proteins/metabolism
Chemical Substances	Adaptor Proteins, Signal Transducing ; Cell Cycle Proteins ; ERC1 protein, human ; Microtubule-Associated Proteins ; Nerve Tissue Proteins ; Phosphoproteins ; spindlin ; MICAL3 protein, human (EC 1.-) ; Mixed Function Oxygenases (EC 1.-) ; RAB8A protein, human (EC 3.6.1.-.) ; rab GTP-Binding Proteins (EC 3.6.5.2)
Language	English
Publishing date	2016-08-15
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	10.1074/jbc.M116.748186
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Article ; Online: Bicaudal d family adaptor proteins control the velocity of Dynein-based movements.

Schlager, Max A / Serra-Marques, Andrea / Grigoriev, Ilya / Gumy, Laura F / Esteves da Silva, Marta / Wulf, Phebe S / Akhmanova, Anna / Hoogenraad, Casper C

Cell reports

2014 Volume 8, Issue 5, Page(s) 1248–1256

Abstract: Cargo transport along microtubules is driven by the collective function of microtubule plus- and minus-end-directed motors (kinesins and dyneins). How the velocity of cargo transport is driven by opposing teams of motors is still poorly understood. Here, ...

Abstract	Cargo transport along microtubules is driven by the collective function of microtubule plus- and minus-end-directed motors (kinesins and dyneins). How the velocity of cargo transport is driven by opposing teams of motors is still poorly understood. Here, we combined inducible recruitment of motors and adaptors to Rab6 secretory vesicles with detailed tracking of vesicle movements to investigate how changes in the transport machinery affect vesicle motility. We find that the velocities of kinesin-based vesicle movements are slower and more homogeneous than those of dynein-based movements. We also find that Bicaudal D (BICD) adaptor proteins can regulate dynein-based vesicle motility. BICD-related protein 1 (BICDR-1) accelerates minus-end-directed vesicle movements and affects Rab6 vesicle distribution. These changes are accompanied by reduced axonal outgrowth in neurons, supporting their physiological importance. Our study suggests that adaptor proteins can modulate the velocity of dynein-based motility and thereby control the distribution of transport carriers.
MeSH term(s)	Adaptor Proteins, Vesicular Transport/metabolism ; Animals ; Axonal Transport ; Cells, Cultured ; Dyneins/metabolism ; HeLa Cells ; Humans ; Kinesin/metabolism ; Microtubule-Associated Proteins/metabolism ; Neurons/metabolism ; Protein Binding ; Protein Transport ; Rats
Chemical Substances	Adaptor Proteins, Vesicular Transport ; Microtubule-Associated Proteins ; Dyneins (EC 3.6.4.2) ; Kinesin (EC 3.6.4.4)
Language	English
Publishing date	2014-09-11
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.2014.07.052
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Article ; Online: BICD2, dynactin, and LIS1 cooperate in regulating dynein recruitment to cellular structures.

Splinter, Daniël / Razafsky, David S / Schlager, Max A / Serra-Marques, Andrea / Grigoriev, Ilya / Demmers, Jeroen / Keijzer, Nanda / Jiang, Kai / Poser, Ina / Hyman, Anthony A / Hoogenraad, Casper C / King, Stephen J / Akhmanova, Anna

Molecular biology of the cell

2012 Volume 23, Issue 21, Page(s) 4226–4241

Abstract: Cytoplasmic dynein is the major microtubule minus-end-directed cellular motor. Most dynein activities require dynactin, but the mechanisms regulating cargo-dependent dynein-dynactin interaction are poorly understood. In this study, we focus on dynein- ... ...

Abstract	Cytoplasmic dynein is the major microtubule minus-end-directed cellular motor. Most dynein activities require dynactin, but the mechanisms regulating cargo-dependent dynein-dynactin interaction are poorly understood. In this study, we focus on dynein-dynactin recruitment to cargo by the conserved motor adaptor Bicaudal D2 (BICD2). We show that dynein and dynactin depend on each other for BICD2-mediated targeting to cargo and that BICD2 N-terminus (BICD2-N) strongly promotes stable interaction between dynein and dynactin both in vitro and in vivo. Direct visualization of dynein in live cells indicates that by itself the triple BICD2-N-dynein-dynactin complex is unable to interact with either cargo or microtubules. However, tethering of BICD2-N to different membranes promotes their microtubule minus-end-directed motility. We further show that LIS1 is required for dynein-mediated transport induced by membrane tethering of BICD2-N and that LIS1 contributes to dynein accumulation at microtubule plus ends and BICD2-positive cellular structures. Our results demonstrate that dynein recruitment to cargo requires concerted action of multiple dynein cofactors.
MeSH term(s)	1-Alkyl-2-acetylglycerophosphocholine Esterase/metabolism ; Carrier Proteins/chemistry ; Carrier Proteins/metabolism ; Dynactin Complex ; Dyneins/metabolism ; HeLa Cells ; Humans ; Membrane Proteins/chemistry ; Membrane Proteins/metabolism ; Microtubule-Associated Proteins/metabolism ; Microtubules/metabolism ; Multiprotein Complexes/metabolism ; Nuclear Envelope/metabolism ; Protein Binding ; Protein Stability ; Protein Transport ; Transport Vesicles/metabolism ; rab GTP-Binding Proteins/metabolism
Chemical Substances	Bicd2 protein, mouse ; Carrier Proteins ; Dynactin Complex ; Membrane Proteins ; Microtubule-Associated Proteins ; Multiprotein Complexes ; 1-Alkyl-2-acetylglycerophosphocholine Esterase (EC 3.1.1.47) ; PAFAH1B1 protein, human (EC 3.1.1.47) ; Dyneins (EC 3.6.4.2) ; rab GTP-Binding Proteins (EC 3.6.5.2)
Language	English
Publishing date	2012-09-05
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	1098979-1
ISSN	1939-4586 ; 1059-1524
ISSN (online)	1939-4586
ISSN	1059-1524
DOI	10.1091/mbc.E12-03-0210
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Article ; Online: Rab6, Rab8, and MICAL3 cooperate in controlling docking and fusion of exocytotic carriers.

Grigoriev, Ilya / Yu, Ka Lou / Martinez-Sanchez, Emma / Serra-Marques, Andrea / Smal, Ihor / Meijering, Erik / Demmers, Jeroen / Peränen, Johan / Pasterkamp, R Jeroen / van der Sluijs, Peter / Hoogenraad, Casper C / Akhmanova, Anna

Current biology : CB

2011 Volume 21, Issue 11, Page(s) 967–974

Abstract: Rab6 is a conserved small GTPase that localizes to the Golgi apparatus and cytoplasmic vesicles and controls transport and fusion of secretory carriers [1]. Another Rab implicated in trafficking from the trans-Golgi to the plasma membrane is Rab8 [2-5]. ... ...

Abstract	Rab6 is a conserved small GTPase that localizes to the Golgi apparatus and cytoplasmic vesicles and controls transport and fusion of secretory carriers [1]. Another Rab implicated in trafficking from the trans-Golgi to the plasma membrane is Rab8 [2-5]. Here we show that Rab8A stably associates with exocytotic vesicles in a Rab6-dependent manner. Rab8A function is not needed for budding or motility of exocytotic carriers but is required for their docking and fusion. These processes also depend on the Rab6-interacting cortical factor ELKS [1], suggesting that Rab8A and ELKS act in the same pathway. We show that Rab8A and ELKS can be linked by MICAL3, a member of the MICAL family of flavoprotein monooxygenases [6]. Expression of a MICAL3 mutant with an inactive monooxygenase domain resulted in a strong accumulation of secretory vesicles that were docked at the cell cortex but failed to fuse with the plasma membrane, an effect that correlated with the strongly reduced mobility of MICAL3. We propose that the monooxygenase activity of MICAL3 is required to regulate its own turnover and the concomitant remodeling of vesicle-docking protein complexes in which it is engaged. Taken together, the results of our study illustrate cooperation of two Rab proteins in constitutive exocytosis and implicates a redox enzyme in this process.
MeSH term(s)	Biological Transport ; Cell Membrane/metabolism ; Cytoplasmic Vesicles/metabolism ; Exocytosis/physiology ; HeLa Cells ; Humans ; Membrane Fusion ; Mixed Function Oxygenases/analysis ; Mixed Function Oxygenases/metabolism ; Mixed Function Oxygenases/physiology ; Oxidation-Reduction ; rab GTP-Binding Proteins/analysis ; rab GTP-Binding Proteins/metabolism ; rab GTP-Binding Proteins/physiology
Chemical Substances	Rab6 protein ; MICAL3 protein, human (EC 1.-) ; Mixed Function Oxygenases (EC 1.-) ; RAB8A protein, human (EC 3.6.1.-.) ; rab GTP-Binding Proteins (EC 3.6.5.2)
Language	English
Publishing date	2011-06-07
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1071731-6
ISSN	1879-0445 ; 0960-9822
ISSN (online)	1879-0445
ISSN	0960-9822
DOI	10.1016/j.cub.2011.04.030
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