Compromise of Clathrin Function and Membrane Association by Clathrin Light Chain Deletion

Wang, Jingshan; Virta, Valerie Christine; Riddelle‐Spencer, Kathryn; O’Halloran, Theresa J.

doi:10.1046/j.1600-0854.2003.00144.x

Cited by 35 publications

(72 citation statements)

References 32 publications

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“…We expressed GFP-Ap2A1 in cells with either disrupted clathrin light chain (clc-) (Wang et al, 2003) or disrupted clathrin heavy chain (chcA-) (Ruscetti et al, 1994). TIR-FM imaging of GFP-Ap2A1 in clc-cells showed that AP2 was able to localize to membrane puncta that behaved with similar dynamics to wild-type cells ( Fig.…”

Section: Intracellular Localization and Dynamics Of Clathrin And Ap2 mentioning

confidence: 99%

“…Genetic deletions of clathrin in Dictyostelium have revealed its importance for macropinocytosis, cytokinesis, development and osmoregulation (O'Halloran and Anderson, 1992;Ruscetti et al, 1994;Niswonger and O'Halloran, 1997a;Niswonger and O'Halloran, 1997b;Wang et al, 2003). Given that clathrin functions at numerous membrane transport steps, it has been difficult to resolve whether CME from the plasma membrane is important for any of these processes.…”

Section: Introductionmentioning

confidence: 99%

“…Osmoregulation phenotypes of varying severity are observed in both clathrin light chain (clc-) (Wang et al, 2003) and heavy chain (chcA-) knockouts (O'Halloran and Anderson, 1992), as well as in knockouts of AP180 (Stavrou and O'Halloran, 2006), the a, b1/2 or m2 subunits of AP2 (Wen et al, 2009;Sosa et al, 2012), and the m1 subunit of AP1 (Lefkir et al, 2003). Although the function of clathrin and its adaptors at the contractile vacuole is unclear, mislocalization of contractile vacuole components in AP1 and AP2 knockouts has suggested roles for these complexes in contractile vacuole biogenesis (Lefkir et al, 2003;Sosa et al, 2012).…”

Section: Introductionmentioning

confidence: 99%

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Dynamics of clathrin-mediated endocytosis and its requirement for organelle biogenesis in Dictyostelium

Macro

Jaiswal

Simon

2012

Journal of Cell Science

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SummaryThe protein clathrin mediates one of the major pathways of endocytosis from the extracellular milieu and plasma membrane. In single-cell eukaryotes, such as Saccharomyces cerevisiae, the gene encoding clathrin is not an essential gene, raising the question of whether clathrin conveys specific advantages for multicellularity. Furthermore, in contrast to mammalian cells, endocytosis in S. cerevisiae is not dependent on either clathrin or adaptor protein 2 (AP2), an endocytic adaptor molecule. In this study, we investigated the requirement for components of clathrin-mediated endocytosis (CME) in another unicellular organism, the amoeba Dictyostelium. We identified a heterotetrameric AP2 complex in Dictyostelium that is similar to that which is found in higher eukaryotes. By simultaneously imaging fluorescently tagged clathrin and AP2, we found that, similar to higher eukaryotes, these proteins colocalized to membrane puncta that move into the cell together. In addition, the contractile vacuole marker protein, dajumin-green fluorescent protein (GFP), is trafficked via the cell membrane and internalized by CME in a clathrin-dependent, AP2-independent mechanism. This pathway is distinct from other endocytic mechanisms in Dictyostelium. Our finding that CME is required for the internalization of contractile vacuole proteins from the cell membrane explains the contractile vacuole biogenesis defect in Dictyostelium cells lacking clathrin. Our results also suggest that the machinery for CME and its role in organelle maintenance appeared early during eukaryotic evolution. We hypothesize that dependence of endocytosis on specific components of the CME pathway evolved later, as demonstrated by internalization independent of AP2 function.

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Section: Intracellular Localization and Dynamics Of Clathrin And Ap2 mentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Dynamics of clathrin-mediated endocytosis and its requirement for organelle biogenesis in Dictyostelium

Macro

Jaiswal

Simon

2012

Journal of Cell Science

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“…Clathrin-deficient Dictyostelium cells show dramatic morphological and functional defects of the CV (O'Halloran and Anderson, 1992;Wang et al, 2003). Deletion of the apm1 gene encoding the medium subunit of the clathrin adaptorprotein AP-1 also results in the absence of a characteristic CV (Lefkir et al, 2003).…”

Section: Introductionmentioning

confidence: 99%

Acidic clusters target transmembrane proteins to the contractile vacuole inDictyosteliumcells

Mercanti

Blanc

Lefkir

et al. 2006

Journal of Cell Science

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The mechanisms responsible for the targeting of transmembrane integral proteins to the contractile vacuole (CV) network in Dictyostelium discoideum are unknown. Here we show that the transfer of the cytoplasmic domain of a CV-resident protein (Rh50) to a reporter transmembrane protein (CsA) is sufficient to address the chimera (CsA-Rh50) to the CV. We identified two clusters of acidic residues responsible for this targeting, and these motifs interacted with the gamma-adaptin AP-1 subunit in a yeast protein-protein interaction assay. For the first time we report the existence of an indirect transport pathway from the plasma membrane to the CV via endosomes. Upon internalization, the small fraction of CsA-Rh50 present at the cell surface was first concentrated in endosomes distinct from early and late p80-positive endosomes and then slowly transported to the CV. Together our results suggest the existence of an AP-1-dependent selective transport to the contractile vacuole in Dictyostelium

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“…Additional work will be needed to sort out whether the position of helix 7j depends at all on the C-terminus of CLC. The fact that CLC knockouts in Saccharomyces cerevisiae destroy the trimeric clathrin structure (70,71), while the clathrin structure in Dicytostelium is unaffected by knocking down CLC (73), suggests that any CLC role will likely be organism specific.…”

Section: Clathrin Detrimerization and Nuclear Localizationmentioning

confidence: 99%

Novel clathrin activity: developments in health and disease

Ybe

2014

Biomolecular Concepts

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Clathrin self-assembles into a coat around vesicles filled with cargo such as nutrients, hormones, and proteins destined for degradation. Recent developments indicate clathrin is not a specialist, but is involved in different processes relevant to health and disease. Clathrin is used to strengthen centrosomes and mitotic spindles essential for chromosome segregation in cell division. In Wnt signaling, clathrin is a component of signalosomes on the plasma membrane needed to produce functional Wnt receptors. In glucose metabolism, a muscle-specific isoform, CHC22 clathrin, is key to the formation of storage compartments for GLUT4 receptor, and CHC22 dysfunction has been tied to type 2 diabetes. The activity of clathrin to self-assemble and to work with huntingtin-interacting proteins to organize actin is exploited by Listeria and enteropathic Escherichia coli in their infection pathways. Finally, there is an important connection between clathrin and human malignancies. Clathrin is argued to help transactivate tumor suppressor p53 that controls specific genes in DNA repair and apoptosis. However, this is debatable because trimeric clathrin must be made monomeric. To get insight on how the clathrin structure could be converted, the crystal structure of the trimerization domain is used in the development of the detrimerization switch hypothesis. This novel hypothesis will be relevant if connections continue to be found between CHC17 and p53 anti-cancer activity in the nucleus.

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Compromise of Clathrin Function and Membrane Association by Clathrin Light Chain Deletion

Cited by 35 publications

References 32 publications

Dynamics of clathrin-mediated endocytosis and its requirement for organelle biogenesis in Dictyostelium

Dynamics of clathrin-mediated endocytosis and its requirement for organelle biogenesis in Dictyostelium

Acidic clusters target transmembrane proteins to the contractile vacuole inDictyosteliumcells

Novel clathrin activity: developments in health and disease

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