The<i>Caenorhabditis elegans</i>JIP3 Protein UNC-16 Functions As an Adaptor to Link Kinesin-1 with Cytoplasmic Dynein

Arimoto, Makoto; Koushika, Sandhya P.; Choudhary, Bikash; Li, Chris; Matsumoto, Kunihiro; Hisamoto, Naoki

doi:10.1523/jneurosci.2653-10.2011

Cited by 93 publications

(121 citation statements)

References 38 publications

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“…Our data with defective kinesin strains show that dynein is actively recruited to the hyphal tips by the action of kinesin motors and that the absence of kinesin prevents dynein from effectively getting to the hyphal tip region. This interpretation of our data is in agreement with work from others that illustrates an essential role for kinesin in the plus-end accumulation of dynein (Brady et al 1990;Echeverri et al 1996;Waterman-Storer et al 1997;Martin et al 1999;Vaughan et al 1999;Duncan and Warrior 2002;Januschke et al 2002;King et al 2003;Zhang et al 2003;Ligon et al 2004;Theiss et al 2005;Lenz et al 2006;Arimoto et al 2011).…”

Section: Discussionsupporting

confidence: 94%

“…The spherical structures were reminiscent of endomembrane organelles that have been described in previous studies (Bowman et al 2009). The short linear tracks resembled the comet tail tip accumulation of dynein at microtubule plus ends that has been reported by studies in other systems ranging from fungi to mammalian neurons (Xiang et al 1995;Vaughan et al 1999;Xiang et al 2000;Han et al 2001;Ma and Chisholm 2002;Lee et al 2003;Sheeman et al 2003;Zhang et al 2003Zhang et al , 2010Zhang et al , 2011Lenz et al 2006;Arimoto et al 2011;Schuster et al 2011a). Apart from the spherical structures and short linear tracks, no additional substructures were visible upon standard exposure settings or photobleaching the bright hyphal tip dynein fluorescence ( Figure S3).…”

Section: Localization Of Dynein Molecules To the Hyphal Tip In N Crasupporting

confidence: 66%

“…This accumulation most likely represents a reservoir of dynein being retained at the hyphal tip for future cargo transport. In addition, wild-type dynein was also found on the ends of microtubules near the hyphal apex in the classic comet-tail structures described in a variety of past studies (Xiang et al 1995(Xiang et al , 2000Vaughan et al 1999;Han et al 2001;Ma and Chisholm 2002;Zhang et al 2003Zhang et al , 2010Zhang et al , 2011Lenz et al 2006;Arimoto et al 2011;Schuster et al 2011a).…”

Section: Discussionmentioning

confidence: 81%

“…Multiple studies have shown that kinesin and dynactin play essential roles in the localization of dynein within cells (Brady et al 1990;Echeverri et al 1996;Waterman-Storer et al 1997;Martin et al 1999;Vaughan et al 1999;Duncan and Warrior 2002;Januschke et al 2002;King et al 2003;Zhang et al 2003;Ligon et al 2004;Theiss et al 2005;Lenz et al 2006;Arimoto et al 2011). To determine if conventional kinesin (Nkin) or dynactin have similar functions in N. crassa, we crossed the DIC-mCherry strain to either a strain carrying repeat-induced point (RIP) mutations in conventional kinesin (Seiler et al 1997) or a dynactin p150 (ro-3) null strain.…”

Section: Dynein Localization Requires Conventional Kinesin and Dynactinmentioning

confidence: 99%

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Analyses of Dynein Heavy Chain Mutations Reveal Complex Interactions Between Dynein Motor Domains and Cellular Dynein Functions

et al. 2012

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Cytoplasmic dynein transports cargoes for a variety of crucial cellular functions. However, since dynein is essential in most eukaryotic organisms, the in-depth study of the cellular function of dynein via genetic analysis of dynein mutations has not been practical. Here, we identify and characterize 34 different dynein heavy chain mutations using a genetic screen of the ascomycete fungus Neurospora crassa, in which dynein is nonessential. Interestingly, our studies show that these mutations segregate into five different classes based on the in vivo localization of the mutated dynein motors. Furthermore, we have determined that the different classes of dynein mutations alter vesicle trafficking, microtubule organization, and nuclear distribution in distinct ways and require dynactin to different extents. In addition, biochemical analyses of dynein from one mutant strain show a strong correlation between its in vitro biochemical properties and the aberrant intracellular function of that altered dynein. When the mutations were mapped to the published dynein crystal structure, we found that the three-dimensional structural locations of the heavy chain mutations were linked to particular classes of altered dynein functions observed in cells. Together, our data indicate that the five classes of dynein mutations represent the entrapment of dynein at five separate points in the dynein mechanochemical and transport cycles. We have developed N. crassa as a model system where we can dissect the complexities of dynein structure, function, and interaction with other proteins with genetic, biochemical, and cell biological studies.T HE organization, survival, and function of eukaryotic cells depend on intracellular transport governed by the microtubule-based molecular motors cytoplasmic dynein and kinesin. Dynein carries out the inward transport of cargos whereas kinesins are responsible for the outward movement. These motors, in addition to the transport and distribution of a wide variety of cargos, are also responsible for vital cellular processes ranging from mitosis to organelle positioning to embryonic development (Schroer et al. 1989;Burkhardt et al. 1997;Rana et al. 2004;Kardon and Vale 2009). Although intracellular transport is necessary for the function of all cells, polarized cells in particular have specific transport needs due to their asymmetry and elongated shape. These extraordinary requirements necessitate efficient longrange microtubule-based transport mechanisms (Hirokawa and Takemura 2005;Zheng et al. 2008;Harada 2010). The anterograde transport needs in these cells are satisfied by a variety of kinesins but only a single cytoplasmic dynein fulfills the retrograde transport requirements.Cytoplasmic dynein is a megadalton-sized, multiprotein complex composed of two heavy chains (DHCs), and varying numbers of dynein intermediate chains (DICs), light intermediate chains, and light chains. The DHCs perform the ATPase motor and microtubule-binding functions and the other subunits couple dynein to dynact...

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Section: Discussionsupporting

confidence: 94%

Section: Localization Of Dynein Molecules To the Hyphal Tip In N Crasupporting

confidence: 66%

Section: Discussionmentioning

confidence: 81%

Section: Dynein Localization Requires Conventional Kinesin and Dynactinmentioning

confidence: 99%

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Analyses of Dynein Heavy Chain Mutations Reveal Complex Interactions Between Dynein Motor Domains and Cellular Dynein Functions

et al. 2012

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“…This effect on axon growth is most likely because of the drastic redistribution of the Rab6 vesicles observed upon BICDR-1 expression from neurite tip to cell soma (74), implying that more than just the velocity of the dynein motors may be affected. Given that JIP3 and JIP1 associate with both kinesin-1 and dynein (41,47,63,75), JIPs may be interesting candidates to elucidate further the signaling modules involved in axon growth control.…”

Section: Figmentioning

confidence: 99%

Signaling Over Distances

Saito

Cavalli

2016

Molecular & Cellular Proteomics

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Neurons are extremely polarized cells. Axon lengths often exceed the dimension of the neuronal cell body by several orders of magnitude. These extreme axonal lengths imply that neurons have mastered efficient mechanisms for long distance signaling between soma and synaptic terminal. These elaborate mechanisms are required for neuronal development and maintenance of the nervous system. Neurons can fine-tune long distance signaling through calcium wave propagation and bidirectional transport of proteins, vesicles, and mRNAs along microtubules. The signal transmission over extreme lengths also ensures that information about axon injury is communicated to the soma and allows for repair mechanisms to be engaged. This review focuses on the different mechanisms employed by neurons to signal over long axonal distances and how signals are interpreted in the soma, with an emphasis on proteomic studies. We also discuss how proteomic approaches could help further deciphering the signaling mechanisms operating over long distance in axons. Neurons have unique and highly polarized morphologies. The axon allows intracellular communication between the cell soma and the distantly located synaptic terminal. The extreme length of axons relative to the cell soma diameter poses great challenges for neuronal development, maintenance, and repair. Anterograde and retrograde axonal transport of proteins vesicles and RNA along the microtubule tracks in the axon is crucial to sustain the required signaling events underlying development and maintenance of the nervous system. The retrograde transport system is also used following axon injury to communicate information from the site of injury back to the soma. Communication between distant axon locations and the cell soma is also ensured by a more rapid signal encoded in calcium waves. Incoming signals from distant axon locations are interpreted by the soma to regulate gene expression for survival or repair. The neuronal epigenome is also influenced by incoming signals to appropriately coordinate transcriptional responses. In this review, we discuss the state of the field regarding the different mechanisms employed by neurons to signal intracellularly over long distances in axons and how signals are interpreted in the cell soma, with an emphasis on proteomic studies. We also discuss how the use of proteomics could further help in understanding long distance signaling system in axons. The communication employed by neurons to signal along dendrites has been reviewed in detail elsewhere (1) and will not be discussed here.Calcium Influx, Back Propagation, and Long Distance Effects-Alterations in axonal calcium levels affect multiple and diverse signaling events, including local protein synthesis and degradation. These local signals can have long distance effects. Axon injury provides a powerful system to study the role of calcium in axonal signaling, because injury-induced calcium influx in the axon triggers important downstream events at the injury site and the soma (Fig.

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JNK‐interacting protein 4 is a central molecule for lysosomal retrograde trafficking

Sasazawa

Saiki

2023

BioEssays

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Lysosomal positioning is an important factor in regulating cellular responses, including autophagy. Because proteins encoded by disease‐responsible genes are involved in lysosomal trafficking, proper intracellular lysosomal trafficking is thought to be essential for cellular homeostasis. In the past few years, the mechanisms of lysosomal trafficking have been elucidated with a focus on adapter proteins linking motor proteins to lysosomes. Here, we outline recent findings on the mechanisms of lysosomal trafficking by focusing on adapter protein c‐Jun NH2‐terminal kinase‐interacting protein (JIP) 4, which plays a central role in this process, and other JIP4 functions and JIP family proteins. Additionally, we discuss neuronal diseases associated with aberrance in the JIP family protein. Accumulating evidence suggests that chemical manipulation of lysosomal positioning may be a therapeutic approach for these neuronal diseases.

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TheCaenorhabditis elegansJIP3 Protein UNC-16 Functions As an Adaptor to Link Kinesin-1 with Cytoplasmic Dynein

Cited by 93 publications

References 38 publications

Analyses of Dynein Heavy Chain Mutations Reveal Complex Interactions Between Dynein Motor Domains and Cellular Dynein Functions

Analyses of Dynein Heavy Chain Mutations Reveal Complex Interactions Between Dynein Motor Domains and Cellular Dynein Functions

Signaling Over Distances

JNK‐interacting protein 4 is a central molecule for lysosomal retrograde trafficking

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