SASDBL2: MBP-PICK1 fusion (Maltose Binding Protein fused to Protein Intera...

Basic information

• Entry: Database: SASBDB / ID: SASDBL2

Sample

MBP-PICK1 fusion

• Maltose Binding Protein fused to Protein Interacting with C kinase 1 (protein), MBP-PICK1, Homo sapiens

Function / homology

Function:

membrane curvature sensor activity / glial cell development / Arp2/3 complex binding / neuronal ion channel clustering / cellular response to decreased oxygen levels / 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 / dendritic spine organization / long-term synaptic depression / dendritic spine maintenance / receptor clustering / positive regulation of receptor internalization / cellular response to glucose starvation / regulation of insulin secretion / protein kinase C binding / trans-Golgi network membrane / Cell surface interactions at the vascular wall / intracellular protein transport / G protein-coupled receptor binding / phospholipid binding / actin filament binding / endocytic vesicle membrane / synaptic vesicle / presynaptic membrane / cytoskeleton / neuron projection / postsynaptic density / protein phosphorylation / protein domain specific binding / signaling receptor binding / synapse / perinuclear region of cytoplasm / Golgi apparatus / metal ion binding / identical protein binding / plasma membrane / cytosol / cytoplasm

Domain/homology:

PICK1, BAR domain / Arfaptin homology (AH) domain / Arfaptin family / Arfaptin-like domain / Arfaptin homology (AH) domain profile. / Arfaptin-like domain / AH/BAR domain superfamily / PDZ domain / PDZ domain profile. / Domain present in PSD-95, Dlg, and ZO-1/2. / PDZ domain / PDZ superfamily

Component:

PRKCA-binding protein

• Biological species: Homo sapiens (human)
• Citation: Journal: Mol Biol Cell / Year: 2015; 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 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.

Contact author

• Roberto Dominguez (Penn, University of Pennsylvania, Philadelphia, PA, United States)

Models

• Model #402: ; Type: dummy / Software: crysol / Radius of dummy atoms: 1.90 A / Chi-square value: 1.1881; Search similar-shape structures of this assembly by Omokage search (details)

Sample

• Sample: Name: MBP-PICK1 fusion / Specimen concentration: 0.46-7.50
• 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 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 / Type of source: X-ray synchrotron
• Detector: Name: Finger Lakes CCD / Type: CCD

Scan

Title: MPP-PICK1 fusion at 3.75mg/ml / Measurement date: Oct 13, 2015 / Cell temperature: 4 °C / Exposure time: 40 sec. / Number of frames: 20 / Unit: 1/nm /

	Min	Max
Q	0.1034	2.9352

Distance distribution function P(R)

Sofotware P(R): GNOM 5.0 / Number of points: 151 /

	Min	Max
Q	0.00790906	0.0991546
P(R) point	1	151
R	0	276

Result

D max: 27.6 / Type of curve: single_conc
Comments: This dataset was collected at a concentration of 3.75 mg/ml.

	Experimental	Porod
MW	172.2 kDa	-
Volume	-	483 nm3

	P(R)	Guinier
Forward scattering, I0	41.58	41.42
Radius of gyration, Rg	8.7 nm	8.38 nm