Novel Function of Clathrin Light Chain in Promoting Endocytic Vesicle Formation

Newpher, Thomas M.; Idrissi, Fatima Zahra; Geli, Maribel; Lemmon, Sandra K.

doi:10.1091/mbc.e06-07-0606

Cited by 41 publications

(55 citation statements)

References 33 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The protein contains the ANTH, coiled-coil, and THATCH domains present in all HIP1 proteins. The coiled-coil domain in Sla2p and HIP1 enables binding to clathrin-light chain, although the exact mode of interaction differs from yeast to mammals, suggesting differences in the regulation of intracellular transport among different species (LegendreGuillemin et al, 2005;Newpher et al, 2006;Ybe et al, 2007).…”

Section: Resultsmentioning

confidence: 99%

See 1 more Smart Citation

Huntingtin-Interacting Protein 1 Influences Worm and Mouse Presynaptic Function and ProtectsCaenorhabditis elegansNeurons against Mutant Polyglutamine Toxicity

Parker¹,

Metzler²,

Georgiou³

et al. 2007

J. Neurosci.

View full text Add to dashboard Cite

Huntingtin-interacting protein 1 (HIP1) was identified through its interaction with htt (huntingtin), the Huntington's disease (HD) protein. HIP1 is an endocytic protein that influences transport and function of AMPA and NMDA receptors in the brain. However, little is known about its contribution to neuronal dysfunction in HD.We report that the Caenorhabditis elegans HIP1 homolog hipr-1 modulates presynaptic activity and the abundance of synaptobrevin, a protein involved in synaptic vesicle fusion. Presynaptic function was also altered in hippocampal brain slices of HIP1 Ϫ/Ϫ mice demonstrating delayed recovery from synaptic depression and a reduction in paired-pulse facilitation, a form of presynaptic plasticity. Interestingly, neuronal dysfunction in transgenic nematodes expressing mutant N-terminal huntingtin was specifically enhanced by hipr-1 loss of function. A similar effect was observed with several other mutant proteins that are expressed at the synapse and involved in endocytosis, such as unc-11/AP180, unc-26/synaptojanin, and unc-57/endophilin.Thus, HIP1 is involved in presynaptic nerve terminal activity and modulation of mutant polyglutamine-induced neuronal dysfunction. Moreover, synaptic proteins involved in endocytosis may protect neurons against amino acid homopolymer expansion.

show abstract

Section: Resultsmentioning

confidence: 99%

“…and KDEQIKN in yeast (Chen and Brodsky, 2005;LegendreGuillemin et al, 2005;Newpher et al, 2006;Ybe et al, 2007). A similar sequence is present in HIPR-1 and corresponds to 458 KDEEITA.…”

Section: Discussionmentioning

confidence: 97%

Huntingtin-Interacting Protein 1 Influences Worm and Mouse Presynaptic Function and ProtectsCaenorhabditis elegansNeurons against Mutant Polyglutamine Toxicity

Parker¹,

Metzler²,

Georgiou³

et al. 2007

J. Neurosci.

View full text Add to dashboard Cite

show abstract

“…Each triskelion is drawn as a "worm" extending from the hook-like representation of the terminal domain on the inside of the shell to the vertex of the triskelion at the outside. by recruitment of HIP1R by the amino-terminal segment of both species (Chen and Brodsky 2005;Newpher et al 2006). …”

Section: Clathrinmentioning

confidence: 99%

Molecular Structure, Function, and Dynamics of Clathrin-Mediated Membrane Traffic

Kirchhausen

Owen

Harrison

2014

Cold Spring Harbor Perspectives in Biology

431

442

View full text Add to dashboard Cite

Clathrin is a molecular scaffold for vesicular uptake of cargo at the plasma membrane, where its assembly into cage-like lattices underlies the clathrin-coated pits of classical endocytosis. This review describes the structures of clathrin, major cargo adaptors, and other proteins that participate in forming a clathrin-coated pit, loading its contents, pinching off the membrane as a lattice-enclosed vesicle, and recycling the components. It integrates as much of the structural information as possible at the time of writing into a sketch of the principal steps in coated-pit and coated-vesicle formation.

show abstract

“…Shared sequences of 22 and 10 residues, respectively, mediate binding to the actin-organizing huntingtin-interacting proteins (mammalian Hip1 and Hip1R, yeast Sla2p) (10)(11)(12) or the leucine-rich repeat kinase 2 (LRRK2) (13). Mammalian cell culture experiments and genetic studies in yeast and flies have shown that, through these interactions, CLCs participate in several pathways that could significantly affect clathrin function in vertebrates.…”

mentioning

confidence: 99%

Clathrin light chains’ role in selective endocytosis influences antibody isotype switching

Majeed

Evans

et al. 2016

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

Clathrin, a cytosolic protein composed of heavy and light chain subunits, assembles into a vesicle coat, controlling receptor-mediated endocytosis. To establish clathrin light chain (CLC) function in vivo, we engineered mice lacking CLCa, the major CLC isoform in B lymphocytes, generating animals with CLC-deficient B cells. In CLCa-null mice, the germinal centers have fewer B cells, and they are enriched for IgA-producing cells. This enhanced switch to IgA production in the absence of CLCa was attributable to increased transforming growth factor β receptor 2 (TGFβR2) signaling resulting from defective endocytosis. Internalization of C-X-C chemokine receptor 4 (CXCR4), but not CXCR5, was affected in CLCa-null B cells, and CLC depletion from cell lines affected endocytosis of the δ-opioid receptor, but not the β2-adrenergic receptor, defining a role for CLCs in the uptake of a subset of signaling receptors. This instance of clathrin subunit deletion in vertebrates demonstrates that CLCs contribute to clathrin’s role in vivo by influencing cargo selectivity, a function previously assigned exclusively to adaptor molecules.

show abstract

Novel Function of Clathrin Light Chain in Promoting Endocytic Vesicle Formation

Cited by 41 publications

References 33 publications

Huntingtin-Interacting Protein 1 Influences Worm and Mouse Presynaptic Function and ProtectsCaenorhabditis elegansNeurons against Mutant Polyglutamine Toxicity

Huntingtin-Interacting Protein 1 Influences Worm and Mouse Presynaptic Function and ProtectsCaenorhabditis elegansNeurons against Mutant Polyglutamine Toxicity

Molecular Structure, Function, and Dynamics of Clathrin-Mediated Membrane Traffic

Clathrin light chains’ role in selective endocytosis influences antibody isotype switching

Contact Info

Product

Resources

About