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Cited by 302Cellular transport and secretionCaveolin-1 and cellular processesBiotin and Related Studies

The DOI matches its Crossref record; 68 of the 68 references it cites were found in a registry or an index; 7 of the 35 sources its claims cite were checked for support.

Disabled‐2 exhibits the properties of a cargo‐selective endocytic clathrin adaptor

Open access
Mishra, Sanjay K., Keyel, Peter A., Hawryluk, Matthew J., Agostinelli, Nicole R., Watkins, Simon C., Traub, Linton M.·2002·The EMBO Journal
DOI 10.1093/emboj/cdf487PMC PMC126284
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Abstract

Clathrin-coated pits at the cell surface select material for transportation into the cell interior. A major mode of cargo selection at the bud site is via the micro 2 subunit of the AP-2 adaptor complex, which recognizes tyrosine-based internalization signals. Other internalization motifs and signals, including phosphorylation and ubiquitylation, also tag certain proteins for incorporation into a coated vesicle, but the mechanism of selection is unclear. Disabled-2 (Dab2) recognizes the FXNPXY internalization motif in LDL-receptor family members via an N-terminal phosphotyrosine-binding (PTB) domain. Here, we show that in addition to binding AP-2, Dab2 also binds directly to phosphoinositides and to clathrin, assembling triskelia into regular polyhedral coats. The FXNPXY motif and phosphoinositides contact different regions of the PTB domain, but can stably anchor Dab2 to the membrane surface, while the distal AP-2 and clathrin-binding determinants regulate clathrin lattice assembly. We propose that Dab2 is a typical member of a growing family of cargo-specific adaptor proteins, including beta-arrestin, AP180, epsin, HIP1 and numb, which regulate clathrin-coat assembly at the plasma membrane by synchronizing cargo selection and lattice polymerization events.

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  3. Reference list68 references found
  4. Reference checkChecking each cited work — 68 of 68
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  6. Claims78 claims anchored to a quote
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Overview

AI snapshot

Written from the paper’s full text.

TL;DR

Dab2 binds AP-2, clathrin, and phosphoinositides, and can assemble clathrin triskelia into polyhedral coats on liposome templates. The authors propose Dab2 is a cargo-selective endocytic adaptor for FXNPXY-bearing cargo such as LDL-receptor family members.

Key findings

  • Dab2’s central region binds AP-2 and clathrin: residues 206–368 are minimal for optimal AP-2 binding, while residues 206–258 bind clathrin; mutation of the type I clathrin-box 236LVDLN to AAALN nearly abolishes clathrin binding in the smallest fragment, and combined LVD→AAA/W→A mutation in 206–368 reduces clathrin binding 4- to 5-fold without affecting AP-2 binding.
  • Dab2 binds preassembled clathrin cages and assembles soluble clathrin trimers into sedimentable polyhedral cages; GST–Dab2(1–368) recruits clathrin, and EM shows regular polyhedral clathrin cages, whereas the minimal clathrin-binding fragment GST–Dab2(206–258) does not increase clathrin recovery above background.
  • The N-terminal PTB domain (residues 1–205) binds phosphoinositides; monomeric PTB binds ~25-fold better to PtdIns(4,5)P2 liposomes, rising from ~2% without phosphoinositide to >50% bound, and can bind phosphoinositides and an LDL-receptor FXNPXY peptide simultaneously.
  • In COS-7 cells, overexpression of myc-Dab2 PTBx2 selectively blocks diI-LDL uptake during a 15 min pulse while transferrin uptake remains normal; in liposome assays, AP-2 plus GST–Dab2 leads to ~50% of total clathrin assembling onto sedimenting liposomes, with ~one-quarter of liposome-bound coat components resistant to 1% Triton X-100.

Methods

  • In vitro binding assays used GST–Dab2 truncations and mutants immobilized on GSH–Sepharose incubated with rat brain cytosol, followed by SDS–PAGE and immunoblotting for AP-2 subunits and clathrin heavy/light chains.
  • Clathrin assembly was tested by mixing purified clathrin with GST–Dab2 fusions, differential centrifugation, negative-stain EM, and liposome/monolayer assays with mixed lipids, phosphoinositides, purified AP-2, and clathrin; Triton X-100 extraction assessed coat assembly.
  • Cell assays included immunofluorescence co-localization of Dab2 and epsin 1 in HeLa cells, and COS-7 transfection with myc-tagged Dab2 PTBx2 followed by diI-LDL and transferrin uptake; siRNA knockdown of Dab2 by >90% in HeLa cells did not inhibit diI-LDL uptake (not shown).

Limitations

  • The paper states no explicit limitations section. It notes that siRNA knockdown of Dab2 by >90% in HeLa cells did not inhibit diI-LDL uptake, that no mutations in Dab2 have been linked to hypercholesterolemia, and that Dab2 is not expressed ubiquitously, with many ovarian and breast carcinomas failing to express it, suggesting possible compensation by other PTB-domain proteins.
  • Evident from the text: many central assembly conclusions rely on in vitro assays with purified proteins and synthetic liposomes; PTBx2 overexpression may not reflect endogenous Dab2 function; some supporting data are “not shown”; and the anti-Dab2 antibody detects all three splice isoforms (p67, p93, p96), so distinct isoform locations cannot be concluded.

Model-written summary. Check it against the paper before relying on it.

Integrity signals

Registry

Crossref · 10.1093/emboj/cdf487

Cites

68 of 68 references verified0 citation errors · 0 not checkable

Statistics

Nothing to recompute.

Verification

Claims the paper makes

7 of 35 cited sources checked · 6 supported · 0 flagged · accuracy not yet measured

  • Findingcitation
    § Dab2 as an endocytic adaptor protein

    Extensive clathrin recruitment does not disrupt the interaction between AP-2 and either Dab2 or epsin, AP180 or HIP1.

    “Importantly, and in contrast to eps15 (Cupers et al., 1998), extensive clathrin recruitment does not disrupt the interaction between AP-2 and either Dab2 or epsin (Figure 8) (Mishra et al., 2001), AP180 (Ford et al., 2001) or HIP1 (Mishra et al., 2001), such that these proteins are now released from the membrane surface.”
    Quote in the paperSubstantial claim1 of 3 sources checked
    • cites Cupers et al., 1998 source
    • cites Mishra et al., 2001 source
    • cites Ford et al., 2001 source
  • Findingown data
    § Dab2 as an endocytic adaptor protein

    Pre-incubating liposomes with a mixture of AP-2 and GST-Dab2 increases the recovery of both proteins in the liposome pellet.

    “Pre-incubating liposomes together with a mixture of AP-2 and the GST±Dab2 fusion increases the recovery of both proteins in the liposome pellet (Figure 8C, lane h), validating the AP-2±Dab2 interactions seen in pull-down assays (Figures 1 and 2) (Morris and Cooper, 2001).”
    Quote in the paperSubstantial claim1 of 1 sources checked
    • cites Morris and Cooper, 2001 source
  • Interpretationcitation
    § Dab2 and cargo recognition

    Dab2 is linked to megalin endocytosis in the kidney in vivo.

    “This links Dab2 to megalin endocytosis in the kidney in vivo.”
    Quote in the paperSubstantial claim1 of 1 sources checked
    • cites Morris et al., 2002b source
  • Premisecitation
    § Dab2 and cargo recognition

    Beta-arrestin appears to accompany heptahelical receptors into existing coated buds.

    “This distinguishes this group of proteins from b-arrestin, which, despite also containing PtdIns(4,5)P 2 -, AP-2-and clathrinbinding determinants, appears to accompany heptahelical receptors into existing coated buds (Santini et al., 2002;Scott et al., 2002).”
    Quote in the paperNot a substantial claim2 of 2 sources checked
    • cites Santini et al., 2002 source
    • cites Scott et al., 2002 source
  • Interpretationreasoning
    § Dab2 and cargo recognition

    Dab2 probably accompanies the clathrin-coated vesicle during budding and fission.

    “These additional functional sequences argue that, like numb (Santolini et al., 2000), Dab2 probably accompanies the clathrin-coated vesicle during budding and ®ssion.”
    Quote in the paperSubstantial claim1 of 1 sources checked
    • cites Santolini et al., 2000 source
  • Probably not a substantial claim. 14
  • It may state two separate claims as one. 12

  • Probably not a substantial claim. The paper’s conclusions may not depend on it.

    Premisecitation
    § Dab2 and cargo recognition

    The CSF-1 receptor utilizes ubiquitin as an endocytic signal.

    “The CSF-1 receptor utilizes ubiquitin as an endocytic signal (Lee et al., 1999), but the NPF triplets in Dab2 could recruit eps15, which, like epsin, can bind ubiquitin directly (Polo et al., 2002).”
    Quote in the paperNot a substantial claim1 of 1 sources checked
    • cites Lee et al., 1999 source

      In “Cbl-targeted CSF-1R multiubiquitination” (page unavailable), the paper reports that CSF-1R is ubiquitinated before endocytosis and suggests that multiubiquitination may promote it. It explicitly says it is unclear whether ubiquitination of Cbl, the receptor, or both is required for internalization, so it does not establish that ubiquitin on CSF-1R serves as the endocytic signal. (LLM, conf=0.88)

      Experimental — accuracy not yet measured

  • It may state two separate claims as one.

    Findingown data
    § Dab2 binds to phosphoinositides via the N-terminal PTB domain

    The Dab2 PTB domain displays a preference for PtdIns(4,5)P2, although there is binding to several phosphoinositides in protein-lipid overlays.

    “Protein±lipid overlays reveal that the Dab2 PTB domain displays a preference for PtdIns(4,5)P 2 , although there is binding to several phosphoinositides in this type of assay (Figure 6C).”
    Quote in the paperSubstantial claim

  • It may state two separate claims as one.

    Findingcitation
    § Dab2 as an endocytic adaptor protein

    Oriented on a 10% PtdIns(4,5)P2-containing monolayer, GST-Dab2(1-368) recruits soluble clathrin and drives the formation of regular polyhedral structures.

    “Oriented in this way upon a 10% PtdIns(4,5)P 2 -containing monolayer of mixed lipids (Ford et al., 2001), the protein is able to recruit soluble clathrin and drive the formation of regular polyhedral structures (Figure 8A and B), which, alone, does not associate with the monolayer (Figure 8A, inset, see C, lane b).”
    Quote in the paperSubstantial claim0 of 1 sources checked
    • cites Ford et al., 2001 source
    • Rests on an assumption: The in vitro assembly of clathrin cages by Dab2 on liposome templates reflects the mechanism of clathrin-coated pit assembly at the plasma membrane.

  • It may state two separate claims as one.

    Findingown data
    § Dab2 binds to phosphoinositides via the N-terminal PTB domain

    In HeLa cells, epsin 1 and Dab2 show extensive co-localization at steady state, indicating that the two proteins are probably present within common clathrin-coated structures.

    “Indeed, in HeLa cells, epsin 1 and Dab2 show extensive co-localization at steady state (Figure 5), indicating that the two proteins are probably present within common clathrin-coated struc-tures.”
    Quote in the paperSubstantial claim

  • It may state two separate claims as one.

    Findingown data
    § Dab2 binds to phosphoinositides via the N-terminal PTB domain

    PTBx2-expressing COS-7 cells are unable to internalize diI-LDL during a 15 min pulse but take up transferrin normally compared with surrounding untransfected cells.

    “PTBx2-expressing cells, unable to internalize diI-LDL during a 15 min pulse, nevertheless take up transferrin normally compared with the surrounding, untransfected cells (Figure 7E±H).”
    Quote in the paperSubstantial claim

  • It may state two separate claims as one.

    Findingown data
    § Results

    Removal of the FXDXF motif has no discernible effect on AP-2 binding, indicating that this sequence is not critical for the alpha-appendage association measured by these assays.

    “Surprisingly, the removal of the FXDXF motif has no discernible effect on AP-2 binding, indicating that this sequence is not critical for the a-appendage association measured by these assays.”
    Quote in the paperSubstantial claim

  • Probably not a substantial claim. The paper’s conclusions may not depend on it.

    Findingown data
    § Immuno¯uorescence analysis

    The intracellular distribution of Dab2 appears to alter with the cell cycle.

    “we note that the intracellular distribution of Dab2 appears to alter with the cell cycle.”
    Quote in the paperNot a substantial claim

  • It may state two separate claims as one.

    Findingown data
    § Immuno¯uorescence analysis

    Dab2 binds to both the AP-2 adaptor complex and clathrin.

    “Dab2 binds to both the AP-2 adaptor complex and clathrin.”
    Quote in the paperSubstantial claim

  • It may state two separate claims as one.

    Findingown data
    § Immuno¯uorescence analysis

    A stable ~25 kDa thrombin degradation product of the Dab2 PTB domain binds phosphoinositides and reacts with anti-Dab2 mAb 52.

    “The asterisk denotes a stable ~25 kDa thrombin degradation product that binds phosphoinositides and reacts with the anti-Dab2 mAb 52.”
    Quote in the paperSubstantial claim

  • It may state two separate claims as one.

    Interpretationreasoning
    § Abstract

    Dab2 is a typical member of a family of cargo-specific adaptor proteins including beta-arrestin, AP180, epsin, HIP1 and numb, which regulate clathrin-coat assembly at the plasma membrane by synchronizing cargo selection and lattice polymerization.

    “We propose that Dab2 is a typical member of a growing family of cargo-speci®c adaptor proteins, including b-arrestin, AP180, epsin, HIP1 and numb, which regulate clathrin-coat assembly at the plasma membrane by synchronizing cargo selection and lattice polymerization events.”
    Quote in the paperSubstantial claim

  • It may state two separate claims as one.

    Interpretationown data
    § Dab2 as an endocytic adaptor protein

    The behavior of GST-Dab2 closely parallels that of GST-epsin 1(1-407) in these assays, showing that Dab2 can function analogously to known endocytic accessory proteins.

    “The behavior of GST±Dab2 closely parallels that of a GST±epsin 1(1±407) fusion in these assays (Figure 8C, lanes k±n), showing that Dab2 can function analogously to known endocytic accessory proteins (Chen et al., 1998;Yamabhai et al., 1998;Drake et al., 2000;Mishra et al., 2001).”
    Quote in the paperSubstantial claim0 of 3 sources checked
    • cites Chen et al., 1998 source
    • cites Yamabhai et al., 1998 source

      Checked before — its earlier verdict is held back until a new check runs.

    • cites Drake et al., 2000 source

      Checked before — its earlier verdict is held back until a new check runs.

  • It may state two separate claims as one.

    Interpretationown data
    § Dab2 interacts directly with clathrin triskelia

    The interaction of Dab2 residues 206-258 with clathrin is largely independent of the AP-2 adaptor complex and may be direct.

    “As little AP-2 binds to the GST±Dab2 (206±258) protein (lanes d), the interaction with clathrin is largely independent of the adaptor complex and may well be direct.”
    Quote in the paperSubstantial claim

  • Probably not a substantial claim. The paper’s conclusions may not depend on it.

    Premisecitation
    § Dab2 and cargo recognition

    Huntingtin has been localized to clathrin-coated structures and endosomes.

    “A potential cargo for HIP1 is huntingtin, which interacts with the N-terminal segment of HIP1 (Wanker et al., 1997) and has been localized to clathrin-coated structures and endosomes (Velier et al., 1998).”
    Quote in the paperNot a substantial claim0 of 1 sources checked
    • cites Velier et al., 1998 source

  • Probably not a substantial claim. The paper’s conclusions may not depend on it.

    Premisecitation
    § Dab2 and cargo recognition

    A potential cargo for HIP1 is huntingtin.

    “A potential cargo for HIP1 is huntingtin, which interacts with the N-terminal segment of HIP1 (Wanker et al., 1997) and has been localized to clathrin-coated structures and endosomes (Velier et al., 1998).”
    Quote in the paperNot a substantial claim0 of 2 sources checked
    • cites Wanker et al., 1997 source
    • cites Velier et al., 1998 source

  • Probably not a substantial claim. The paper’s conclusions may not depend on it.

    Premisecitation
    § Dab2 and cargo recognition

    Epsin might be part of the machinery that recognizes ubiquitin as an endocytic signal.

    “Epsin might be part of the long-sought-after machinery that recognizes ubiquitin as an endocytic signal (Polo et al., 2002).”
    Quote in the paperNot a substantial claim0 of 1 sources checked
    • cites Polo et al., 2002 source

  • Probably not a substantial claim. The paper’s conclusions may not depend on it.

    Premisecitation
    § Dab2 and cargo recognition

    Huntingtin interacts with the N-terminal segment of HIP1.

    “A potential cargo for HIP1 is huntingtin, which interacts with the N-terminal segment of HIP1 (Wanker et al., 1997) and has been localized to clathrin-coated structures and endosomes (Velier et al., 1998).”
    Quote in the paperNot a substantial claim0 of 1 sources checked
    • cites Wanker et al., 1997 source

  • Probably not a substantial claim. It may be too vague to check against evidence. The paper’s conclusions may not depend on it.

    Interpretationreasoning
    § Dab2 and cargo recognition

    These multifaceted connections may be a critical aspect of ensuring the fidelity of cargo incorporation into assembling coated buds.

    “These multifaceted connections may be a critical aspect of ensuring the ®delity of cargo incorporation into assembling coated buds.”
    Quote in the paperNot a substantial claim

  • Probably not a substantial claim. The paper’s conclusions may not depend on it.

    Premisecitation
    § Dab2 and cargo recognition

    Dab2 was initially identified as a prominent phosphoprotein accompanying CSF-1 receptor activation.

    “The protein was initially identi®ed as a prominent phosphoprotein accompanying colony-stimulating factor-1 (CSF-1) receptor activation (Xu et al., 1995).”
    Quote in the paperNot a substantial claim0 of 1 sources checked
    • cites Xu et al., 1995

      Couldn’t be matched to a paper in Crossref, so it can’t be checked.

  • Probably not a substantial claim. The paper’s conclusions may not depend on it.

    Premisecitation
    § Dab2 and cargo recognition

    Eps15 can bind ubiquitin directly.

    “The CSF-1 receptor utilizes ubiquitin as an endocytic signal (Lee et al., 1999), but the NPF triplets in Dab2 could recruit eps15, which, like epsin, can bind ubiquitin directly (Polo et al., 2002).”
    Quote in the paperNot a substantial claim0 of 1 sources checked
    • cites Polo et al., 2002 source

  • Probably not a substantial claim. The paper’s conclusions may not depend on it.

    Premisecitation
    § Dab2 and cargo recognition

    Mammalian EH domain-containing proteins include eps15, intersectin, POB-1 and EHD1.

    “Mammalian EH domain-containing proteins include eps15, intersectin, POB-1 and EHD1 (Santolini et al., 1999).”
    Quote in the paperNot a substantial claim0 of 1 sources checked
    • cites Santolini et al., 1999 source

  • It may state two separate claims as one.

    Interpretationown data
    § Dab2 and cargo recognition

    Other PTB domain proteins might compensate or substitute for Dab2 loss, and thus Dab2 would not be singularly responsible for LDL receptor incorporation into clathrin-coated vesicles.

    “This suggests that other PTB domain proteins might compensate or substitute for Dab2 loss, and thus Dab2 would not be singularly responsible for LDL receptor incorporation into clathrincoated vesicles.”
    Quote in the paperSubstantial claim

  • It may state two separate claims as one.

    Premisecitation
    § Dab2 and cargo recognition

    Dab2 is implicated in TGF-beta receptor activation and downstream Smad activation.

    “Dab2 is also implicated in transforming growth factor b (TGF-b) receptor activation and downstream Smad activation (Hocevar et al., 2001).”
    Quote in the paperNot a substantial claim0 of 1 sources checked
    • cites Hocevar et al., 2001 source

      Checked before — its earlier verdict is held back until a new check runs.

  • Probably not a substantial claim. The paper’s conclusions may not depend on it.

    Interpretationreasoning
    § Dab2 and cargo recognition

    Dab2 may also determine vesicle size.

    “Rather, like epsin and AP180, it potentiates AP-2-driven coat formation, perhaps also determining vesicle size.”
    Quote in the paperNot a substantial claim

  • Probably not a substantial claim. The paper’s conclusions may not depend on it.

    Premisecitation
    § Dab2 and cargo recognition

    AP180 could actively cluster synaptobrevin/VAMP.

    “AP180 could actively cluster synaptobrevin/VAMP (Nonet et al., 1999).”
    Quote in the paperNot a substantial claim0 of 1 sources checked
    • cites Nonet et al., 1999 source

      Checked before — its earlier verdict is held back until a new check runs.

  • Probably not a substantial claim. The paper’s conclusions may not depend on it.

    Interpretationcitation
    § Dab2 and cargo recognition

    The NPF triplets in Dab2 could recruit eps15.

    “The CSF-1 receptor utilizes ubiquitin as an endocytic signal (Lee et al., 1999), but the NPF triplets in Dab2 could recruit eps15, which, like epsin, can bind ubiquitin directly (Polo et al., 2002).”
    Quote in the paperNot a substantial claim

  • Probably not a substantial claim.

    Premisecitation
    § Dab2 and cargo recognition

    Smad2 and Smad3 activation by liganded TGF-beta receptors occurs only post-endocytic internalization.

    “Intriguingly, Smad2 and Smad3 activation by liganded TGF-b receptors occurs only post-endocytic internalization (Penheiter et al., 2002), raising the possibility that Dab2, acting at the coated vesicle, coordinates aspects of TGF-b signaling.”
    Quote in the paperSubstantial claim0 of 1 sources checked
    • cites Penheiter et al., 2002 source
26 of 26

  • The paper relies on this without support.

    The in vitro assembly of clathrin cages by Dab2 on liposome templates reflects the mechanism of clathrin-coated pit assembly at the plasma membrane.

    “With synthetic liposome templates, Dab2 drives clathrin-coat assembly in the presence of puri®ed AP-2 and clathrin and, consequently, displays all the properties of a cargo-speci®c adaptor protein.”

  • The paper relies on this without support.

    The LDL receptor cytosolic domain peptide used in binding assays represents the intact LDL receptor's FXNPXY internalization motif.

    “Addition of a 3-to 5-fold molar excess of a peptide corresponding to residues 2±22 of the LDL receptor cytosolic domain ( 814 NWRLKNINSIFDNPVYQKTT) does not diminish the extent of monomeric PTB domain association with the liposomes (Figure 6D, lane d compared with b).”
2 of 2

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Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

Each contradiction between two passages listed here was confirmed by an independent check.

  • Figure 6 caption names a different internalization motif

    Minor

    The Figure 6D caption says the PTB domain binds FXNPXF motifs, whereas the text identifies the motif as FXNPXY. The peptide tested in that figure also contains the FXNPXY sequence.

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Metadata

Authors
Mishra, S. K., Keyel, P. A., Hawryluk, M. J., Agostinelli, N. R., Watkins, S. C., & Traub, L. M.
Affiliations
University of Pittsburgh (US)
Corresponding author
Traub, Linton M.
ORCID
Venue
The EMBO Journal
Publisher
Springer Science and Business Media LLC
Published
2002-09-16
Volume
21
Issue
18
Pages
4915-4926
ISSN
  • 0261-4189 (ISSN-L)
  • 1460-2075
DOI
10.1093/emboj/cdf487
PMC
PMC126284
OpenAlex
W1983921682
Semantic Scholar
f2627d366f380de384fe68eee4a251f9a7898e0d
Cited by
302
References
68
Citations by year
2026: 4 · 2025: 4 · 2024: 2 · 2023: 1 · 2022: 8 · 2021: 10 · 2020: 6 · 2019: 5 · 2018: 4 · 2017: 5 · 2016: 8 · 2015: 15 · 2014: 10 · 2013: 16 · 2012: 12
FWCI
7.14
Type
journal article
Language
en
Open access
Licence
Locations
  • The EMBO Journal (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
Funders
  • National Institutes of Health
  • National Institute of Diabetes and Digestive and Kidney Diseases (R01DK053249)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Caveolin-1 and cellular processes
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Biotin and Related Studies
Keywords
Disabled-2, clathrin adaptor proteins, clathrin-coated pits, cargo selection, phosphoinositides, phosphotyrosine binding domain, AP-2, membrane internalization, clathrin-coated vesicles
MeSH terms
Amino Acid Sequence, Animals, Biological Transport, Carrier Proteins, Clathrin, Endocytosis, Fluorescent Dyes, HeLa Cells, Humans, Molecular Sequence Data, Neuropeptides, Peptides, Phosphatidylinositols, Protein Binding, Proteins, Receptors, LDL, Recombinant Fusion Proteins, Genes, Tumor Suppressor, Genes, Reporter, COS Cells, Amino Acid Motifs, Tumor Suppressor Proteins, Vesicular Transport Proteins, Adaptor Proteins, Vesicular Transport, Adaptor Protein Complex 2, Adaptor Proteins, Signal Transducing, Apoptosis Regulatory Proteins, Mice

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