HIP1 Functions in Clathrin-mediated Endocytosis through Binding to Clathrin and Adaptor Protein 2

Metzler, Martina; Legendre-Guillemin, Valerie; Gan, Lu; Chopra, Vikramjit; Kwok, Anita; McPherson, Peter S.; Hayden, Michael R.

doi:10.1074/jbc.c100401200

Cited by 183 publications

(183 citation statements)

References 33 publications

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“…GST-ENTH MP90 (amino acids 1-137) (33) and GST-ENTH Af10 (amino acids 1-153) (3) were amplified by PCR using full-length cDNA templates and cloned between the EcoRI and BamHI sites of pGEX-2TK (Amersham Biosciences). GST-HIP1-ANTH (amino acids 1-125) and GST-HIP12-ANTH (amino acids 1-150) expression constructs were generated by PCR amplification from their respective full-length cDNAs (20,34), followed by cloning into the pGEX-6P vector (Amersham Biosciences). The 3Ј-end of each HIP construct was tagged with codons for three glycines followed by six histidine residues and a stop codon.…”

Section: Methodsmentioning

confidence: 99%

A Role for Epsin N-terminal Homology/AP180 N-terminal Homology (ENTH/ANTH) Domains in Tubulin Binding

Hussain

Yamabhai

Bhakar

et al. 2003

Journal of Biological Chemistry

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The epsin N-terminal homology (ENTH) domain is a protein module of ϳ150 amino acids found at the N terminus of a variety of proteins identified in yeast, plants, nematode, frog, and mammals. ENTH domains comprise multiple ␣-helices folded upon each other to form a compact globular structure that has been implicated in interactions with lipids and proteins. In characterizing this evolutionarily conserved domain, we isolated and identified tubulin as an ENTH domain-binding partner. The interaction, which is direct and has a dissociation constant of ϳ1 M, was observed with ENTH domains of proteins present in various species. Tubulin is co-immunoprecipitated from rat brain extracts with the ENTH domain-containing proteins, epsins 1 and 2, and punctate epsin staining is observed along the microtubule cytoskeleton of dissociated cortical neurons. Consistent with a role in microtubule processes, the over-expression of epsin ENTH domain in PC12 cells stimulates neurite outgrowth. These data demonstrate an evolutionarily conserved property of ENTH domains to interact with tubulin and microtubules.The epsin N-terminal homology (ENTH) 1 domain is an evolutionarily conserved globular module of ϳ150 amino acids that occurs at the amino terminus of a variety of proteins (1, 2).Originally noted in the plant protein, Af10 (3), the ENTH domain has subsequently been characterized in epsins (2) and enthoprotin (4) (also termed epsinR (5, 6) or Clint (7)), and in yeast proteins including Ent1p/Ent2p (8, 9) and Ent3p (10). Adaptor protein 180 (AP180), clathrin assembly lymphoid myeloid leukemia protein (CALM), Huntingtin-interacting protein-1 (HIP1) and HIP12, and the yeast proteins yAP180 and Sla2p contain a module that is so similar in structure to the epsin ENTH domain that they were initially denoted ENTHbearing proteins (11-13). However, recent structural studies have refined our understanding such that ENTH-like domains from these proteins have been re-designated ANTH domaincontaining proteins in accordance with their higher structural similarity to AP180 rather than epsin (14). In an effort to simplify the nomenclature applied in this study, we refer to these homologous structures as E/ANTH domains when collectively discussing proteins bearing either domain, but maintain the ENTH or ANTH nomenclature when discussing individual proteins.A common feature among many E/ANTH domain-bearing proteins is that their C termini contain peptide motifs, indicative of a functional role in clathrin-mediated membrane budding including clathrin and clathrin adaptor protein-binding elements (1,15). In addition to their interactions with multiple endocytic components, many of the currently characterized E/ANTH proteins, including epsin, AP180, and HIP1/12, are localized to clathrin-coated pits where they function in clathrin-mediated endocytosis (2, 16 -25). Interestingly, enthoprotin is unique in this group because it is predominantly localized to the trans-Golgi network rather than the plasma membrane, and it appears to regulate clathrin-medi...

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Section: Methodsmentioning

confidence: 99%

A Role for Epsin N-terminal Homology/AP180 N-terminal Homology (ENTH/ANTH) Domains in Tubulin Binding

Hussain

Yamabhai

Bhakar

et al. 2003

Journal of Biological Chemistry

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“…Two other proteins that contain ENTH domains, HIP1 and HIP1R, and their counterpart in S. cerevisiae, Sla2p, interact with the actin cytoskeleton as well as play a role in endocytosis (95,232,238,369,383,401). Phosphatidylinositides play a major role in regulating actin (404), and the ENTH domains of HIP1 and HIP1R may function to coordinate the assembly of endocytic coat proteins with changes in the actin cytoskeleton.…”

Section: Enth/anth Domainsmentioning

confidence: 99%

Phosphoinositides in Constitutive Membrane Traffic

Roth

2004

Physiological Reviews

263

267

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Proteins that make, consume, and bind to phosphoinositides are important for constitutive membrane traffic. Different phosphoinositides are concentrated in different parts of the central vacuolar pathway, with phosphatidylinositol 4-phosphate predominate on Golgi, phosphatidylinositol 4,5-bisphosphate predominate at the plasma membrane, phosphatidylinositol 3-phosphate the major phosphoinositide on early endosomes, and phosphatidylinositol 3,5-bisphosphate found on late endocytic organelles. This spatial segregation may be the mechanism by which the direction of membrane traffic is controlled. Phosphoinositides increase the affinity of membranes for peripheral membrane proteins that function for sorting protein cargo or for the docking and fusion of transport vesicles. This implies that constitutive membrane traffic may be regulated by the mechanisms that control the activity of the enzymes that produce and consume phosphoinositides. Although the lipid kinases and phosphatases that function in constitutive membrane traffic are beginning to be identified, their regulation is poorly understood.

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“…Hip1 is closely related to Hip1R (ϳ50% overall amino acid sequence identity) and has been implicated in the pathology of Huntington disease (Kalchman et al, 1997;Wanker et al, 1997). Similar to Hip1R, Hip1 has been shown to be enriched in CCVs, to colocalize with markers for receptor-mediated endocytosis, and to bind to other endocytic proteins (clathrin, AP-2; Metzler et al, 2001;Mishra et al, 2001;Waelter et al, 2001;Legendre-Guillemin et al, 2002). Recently, phenotypic analysis of Hip1 knockout mice suggested that Hip1 functions in receptor-mediated endocytosis (Metzler et al, 2003), similar to its yeast homologue, Sla2p.…”

Section: Introductionmentioning

confidence: 99%

RNAi-mediated Hip1R Silencing Results in Stable Association between the Endocytic Machinery and the Actin Assembly Machinery

Engqvist-Goldstein

Zhang

Carréno

et al. 2004

MBoC

144

157

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Actin filaments transiently associate with the endocytic machinery during clathrin-coated vesicle formation. Although several proteins that might mediate or regulate this association have been identified, in vivo demonstration of such an activity has not been achieved. Huntingtin interacting protein 1R (Hip1R) is a candidate cytoskeletal-endocytic linker or regulator because it binds to clathrin and actin. Here, Hip1R levels were lowered by RNA interference (RNAi). Surprisingly, rather than disrupting the transient association between endocytic and cytoskeletal proteins, clathrin-coated structures (CCSs) and their endocytic cargo became stably associated with dynamin, actin, the Arp2/3 complex, and its activator, cortactin. RNAi double-depletion experiments demonstrated that accumulation of the cortical actin-endocytic complexes depended on cortactin. Fluorescence recovery after photobleaching showed that dynamic actin filament assembly can occur at CCSs. Our results provide evidence that Hip1R helps to make the interaction between actin and the endocytic machinery functional and transient.

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HIP1 Functions in Clathrin-mediated Endocytosis through Binding to Clathrin and Adaptor Protein 2

Cited by 183 publications

References 33 publications

A Role for Epsin N-terminal Homology/AP180 N-terminal Homology (ENTH/ANTH) Domains in Tubulin Binding

A Role for Epsin N-terminal Homology/AP180 N-terminal Homology (ENTH/ANTH) Domains in Tubulin Binding

Phosphoinositides in Constitutive Membrane Traffic

RNAi-mediated Hip1R Silencing Results in Stable Association between the Endocytic Machinery and the Actin Assembly Machinery

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