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- SASDBL2: MBP-PICK1 fusion (Maltose Binding Protein fused to Protein Intera... -
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Open data
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Basic information
Entry | Database: SASBDB / ID: SASDBL2 |
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![]() | MBP-PICK1 fusion
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Function / homology | ![]() membrane curvature sensor activity / postsynaptic early endosome / glial cell development / neuronal ion channel clustering / cellular response to decreased oxygen levels / Arp2/3 complex binding / Trafficking of GluR2-containing AMPA receptors / regulation of Arp2/3 complex-mediated actin nucleation / negative regulation of Arp2/3 complex-mediated actin nucleation / monoamine transport ...membrane curvature sensor activity / postsynaptic early endosome / glial cell development / neuronal ion channel clustering / cellular response to decreased oxygen levels / Arp2/3 complex binding / Trafficking of GluR2-containing AMPA receptors / regulation of Arp2/3 complex-mediated actin nucleation / negative regulation of Arp2/3 complex-mediated actin nucleation / monoamine transport / : / retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum / dendritic spine organization / long-term synaptic depression / dendritic spine maintenance / receptor clustering / regulation of insulin secretion / positive regulation of receptor internalization / cellular response to glucose starvation / trans-Golgi network membrane / G protein-coupled receptor binding / Cell surface interactions at the vascular wall / protein kinase C binding / intracellular protein transport / phospholipid binding / endocytic vesicle membrane / actin filament binding / synaptic vesicle / presynaptic membrane / postsynaptic density / cytoskeleton / neuron projection / protein domain specific binding / protein phosphorylation / signaling receptor binding / synapse / perinuclear region of cytoplasm / Golgi apparatus / identical protein binding / metal ion binding / plasma membrane / cytosol / cytoplasm Similarity search - Function |
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![]() | ![]() Title: PICK1 is implicated in organelle motility in an Arp2/3 complex-independent manner. Authors: Yadaiah Madasu / Changsong Yang / Malgorzata Boczkowska / Kelley A Bethoney / Adam Zwolak / Grzegorz Rebowski / Tatyana Svitkina / Roberto Dominguez / ![]() Abstract: PICK1 is a modular scaffold implicated in synaptic receptor trafficking. It features a PDZ domain, a BAR domain, and an acidic C-terminal tail (ACT). Analysis by small- angle x-ray scattering ...PICK1 is a modular scaffold implicated in synaptic receptor trafficking. It features a PDZ domain, a BAR domain, and an acidic C-terminal tail (ACT). Analysis by small- angle x-ray scattering suggests a structural model that places the receptor-binding site of the PDZ domain and membrane-binding surfaces of the BAR and PDZ domains adjacent to each other on the concave side of the banana-shaped PICK1 dimer. In the model, the ACT of one subunit of the dimer interacts with the PDZ and BAR domains of the other subunit, possibly accounting for autoinhibition. Consistently, full-length PICK1 shows diffuse cytoplasmic localization, but it clusters on vesicle-like structures that colocalize with the trans-Golgi network marker TGN38 upon deletion of either the ACT or PDZ domain. This localization is driven by the BAR domain. Live-cell imaging further reveals that PICK1-associated vesicles undergo fast, nondirectional motility in an F-actin-dependent manner, but deleting the ACT dramatically reduces vesicle speed. Thus the ACT links PICK1-associated vesicles to a motility factor, likely myosin, but, contrary to previous reports, PICK1 neither binds nor inhibits Arp2/3 complex. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
-Data source
SASBDB page | ![]() |
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-Related structure data
Similar structure data |
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External links
Related items in Molecule of the Month |
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-Models
Model #402 | ![]() Type: dummy / Software: crysol / Radius of dummy atoms: 1.90 A / Chi-square value: 1.1881 ![]() |
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Sample
![]() | Name: MBP-PICK1 fusion / Specimen concentration: 0.46-7.50 |
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Buffer | Name: 50 mM Tris / pH: 7.5 / Composition: 300 mM NaCl, 1 mM maltose, 1 mM EGTA, 2 mM DTT |
Entity #266 | Name: MBP-PICK1 / Type: protein Description: Maltose Binding Protein fused to Protein Interacting with C kinase 1 Formula weight: 87.089 / Num. of mol.: 2 / Source: Homo sapiens / References: UniProt: Q9NRD5 Sequence: MKIEEGKLVI WINGDKGYNG LAEVGKKFEK DTGIKVTVEH PDKLEEKFPQ VAATGDGPDI IFWAHDRFGG YAQSGLLAEI TPDKAFQDKL YPFTWDAVRY NGKLIAYPIA VEALSLIYNK DLLPNPPKTW EEIPALDKEL KAKGKSALMF NLQEPYFTWP LIAADGGYAF ...Sequence: MKIEEGKLVI WINGDKGYNG LAEVGKKFEK DTGIKVTVEH PDKLEEKFPQ VAATGDGPDI IFWAHDRFGG YAQSGLLAEI TPDKAFQDKL YPFTWDAVRY NGKLIAYPIA VEALSLIYNK DLLPNPPKTW EEIPALDKEL KAKGKSALMF NLQEPYFTWP LIAADGGYAF KYENGKYDIK DVGVDNAGAK AGLTFLVDLI KNKHMNADTD YSIAEAAFNK GETAMTINGP WAWSNIDTSK VNYGVTVLPT FKGQPSKPFV GVLSAGINAA SPNKELAKEF LENYLLTDEG LEAVNKDKPL GAVALKSYEE ELAKDPRIAA TMENAQKGEI MPNIPQMSAF WYAVRTAVIN AASGRQTVDA ALAAAQTNAA AMFADLDYDI EEDKLGIPTV PGKVTLQKDA QNLIGISIGG GAQYCPCLYI VQVFDNTPAA LDGTVAAGDE ITGVNGRSIK GKTKVEVAKM IQEVKGEVTI HYNKLQADPK QGMSLDIVLK KVKHRLVENM SSGTADALGL SRAILCNDGL VKRLEELERT AELYKGMTEH TKNLLRAFYE LSQTHRAFGD VFSVIGVREP QPAASEAFVK FADAHRSIEK FGIRLLKTIK PMLTDLNTYL NKAIPDTRLT IKKYLDVKFE YLSYCLKVKE MDDEEYSCIA LGEPLYRVST GNYEYRLILR CRQEARARFS QMRKDVLEKM ELLDQKHVQD IVFQLQRLVS TMSKYYNDCY AVLRDADVFP IEVDLAHTTL AYGLNQEEFT DGEEEEEEED TAAGEPSRDT RGAAGPLDKG GSWCDS |
-Experimental information
Beam | Instrument name: Cornell High Energy Synchrotron Source (CHESS) G1 City: Ithaca, NY / 国: USA ![]() | ||||||||||||||||||
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Detector | Name: Finger Lakes CCD / Type: CCD | ||||||||||||||||||
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Distance distribution function P(R) |
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Result | Comments: This dataset was collected at a concentration of 3.75 mg/ml.
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