Hold the door: hPMCA1/neuroplastin interactions regulate Ca2+-binding site accessibility

Christina K. Go; Jonathan Soboloff

doi:10.1016/j.ceca.2018.10.003

Hold the door: hPMCA1/neuroplastin interactions regulate Ca²⁺-binding site accessibility

Christina K. Go, Jonathan Soboloff

Temple University

Research output: Contribution to journal › Comment/debate

7 Scopus citations

Abstract

In a September 2018 paper published in Nature Communications, Gong et al. identified the domains through which human PMCA1 and neuroplastin (NPTN) interact. Upon binding, hPMCA1 TM domains separate T110 in TM1 and A370 in TM3 to reveal the Ca²⁺-binding site. Thus, NPTN is able to directly modulate the accessibility of cytosolic Ca²⁺ to PMCA.

Original language	English
Pages (from-to)	135-136
Number of pages	2
Journal	Cell Calcium
Volume	76
DOIs	https://doi.org/10.1016/j.ceca.2018.10.003
State	Published - Dec 2018

Keywords

Binding Sites
Calcium
Cell Membrane
Humans
Membrane Glycoproteins
Plasma Membrane Calcium-Transporting ATPases
Protein Domains

Access to Document

10.1016/j.ceca.2018.10.003

Cite this

@article{cdec1423fea6455f96d19ad7f717cbc7,

title = "Hold the door: hPMCA1/neuroplastin interactions regulate Ca2+-binding site accessibility",

abstract = "In a September 2018 paper published in Nature Communications, Gong et al. identified the domains through which human PMCA1 and neuroplastin (NPTN) interact. Upon binding, hPMCA1 TM domains separate T110 in TM1 and A370 in TM3 to reveal the Ca2+-binding site. Thus, NPTN is able to directly modulate the accessibility of cytosolic Ca2+ to PMCA.",

keywords = "Binding Sites, Calcium, Cell Membrane, Humans, Membrane Glycoproteins, Plasma Membrane Calcium-Transporting ATPases, Protein Domains",

author = "Go, {Christina K.} and Jonathan Soboloff",

year = "2018",

month = dec,

doi = "10.1016/j.ceca.2018.10.003",

language = "English",

volume = "76",

pages = "135--136",

journal = "Cell Calcium",

issn = "0143-4160",

publisher = "Elsevier Ltd.",

}

TY - JOUR

T1 - Hold the door

T2 - hPMCA1/neuroplastin interactions regulate Ca2+-binding site accessibility

AU - Go, Christina K.

AU - Soboloff, Jonathan

PY - 2018/12

Y1 - 2018/12

N2 - In a September 2018 paper published in Nature Communications, Gong et al. identified the domains through which human PMCA1 and neuroplastin (NPTN) interact. Upon binding, hPMCA1 TM domains separate T110 in TM1 and A370 in TM3 to reveal the Ca2+-binding site. Thus, NPTN is able to directly modulate the accessibility of cytosolic Ca2+ to PMCA.

AB - In a September 2018 paper published in Nature Communications, Gong et al. identified the domains through which human PMCA1 and neuroplastin (NPTN) interact. Upon binding, hPMCA1 TM domains separate T110 in TM1 and A370 in TM3 to reveal the Ca2+-binding site. Thus, NPTN is able to directly modulate the accessibility of cytosolic Ca2+ to PMCA.

KW - Binding Sites

KW - Calcium

KW - Cell Membrane

KW - Humans

KW - Membrane Glycoproteins

KW - Plasma Membrane Calcium-Transporting ATPases

KW - Protein Domains

UR - http://www.scopus.com/inward/record.url?scp=85055903348&partnerID=8YFLogxK

U2 - 10.1016/j.ceca.2018.10.003

DO - 10.1016/j.ceca.2018.10.003

M3 - Comment/debate

C2 - 30401481

SN - 0143-4160

VL - 76

SP - 135

EP - 136

JO - Cell Calcium

JF - Cell Calcium

ER -

Hold the door: hPMCA1/neuroplastin interactions regulate Ca²⁺-binding site accessibility

Abstract

Keywords

Access to Document

Other files and links

Fingerprint

Cite this