Analysis of proteins interacting with TRIP8b adapter

N. V. Popova; A. N. Plotnikov; R. Kh Ziganshin; I. E. Deyev; A. G. Petrenko

doi:10.1134/S0006297908060035

Analysis of proteins interacting with TRIP8b adapter

N. V. Popova, A. N. Plotnikov, R. Kh Ziganshin, I. E. Deyev, A. G. Petrenko

Research output: Contribution to journal › Article › peer-review

15 Scopus citations

Abstract

Calcium-independent receptor of latrotoxin (CIRL) is an orphan heptahelical receptor implicated in regulation of exocytosis. To characterize molecular mechanisms of CIRL functioning, we searched for its intracellular partners using the yeast two-hybrid SR system with the cytoplasmic C-terminal fragment of CIRL as bait. One of the interacting proteins was identified as TRIP8b, a putative cytosolic adapter protein with multiple tetratricopeptide repeats. To understand functional significance of CIRL-TRIP8b interaction, we further isolated TRIP8b-interacting proteins by affinity chromatography of brain extracts on immobilized recombinant TRIP8b. Sixteen proteins were identified by mass spectrometry in the purified preparations. Clathrin and subunits of AP2 complex appeared to be the major TRIP8b-interacting proteins. Our data suggest a role of TRIP8b in receptor-mediated endocytosis.

Original language	English
Pages (from-to)	644-651
Number of pages	8
Journal	Biochemistry (Moscow)
Volume	73
Issue number	6
DOIs	https://doi.org/10.1134/S0006297908060035
State	Published - Jun 2008
Externally published	Yes

Keywords

CIRL/latrophilin
Clathrin
Endocytosis
TRIP8b

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10.1134/S0006297908060035

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@article{57a3ff562bd44a20900e61fd7985069c,

title = "Analysis of proteins interacting with TRIP8b adapter",

abstract = "Calcium-independent receptor of latrotoxin (CIRL) is an orphan heptahelical receptor implicated in regulation of exocytosis. To characterize molecular mechanisms of CIRL functioning, we searched for its intracellular partners using the yeast two-hybrid SR system with the cytoplasmic C-terminal fragment of CIRL as bait. One of the interacting proteins was identified as TRIP8b, a putative cytosolic adapter protein with multiple tetratricopeptide repeats. To understand functional significance of CIRL-TRIP8b interaction, we further isolated TRIP8b-interacting proteins by affinity chromatography of brain extracts on immobilized recombinant TRIP8b. Sixteen proteins were identified by mass spectrometry in the purified preparations. Clathrin and subunits of AP2 complex appeared to be the major TRIP8b-interacting proteins. Our data suggest a role of TRIP8b in receptor-mediated endocytosis.",

keywords = "CIRL/latrophilin, Clathrin, Endocytosis, TRIP8b",

author = "Popova, {N. V.} and Plotnikov, {A. N.} and Ziganshin, {R. Kh} and Deyev, {I. E.} and Petrenko, {A. G.}",

note = "Funding Information: This work was financially supported by the Russian Foundation for Basic Research (grant No. 06 04 49706a), Fundamental Sciences for Medicine and Molecular and Cellular Biology Programs of Presidium of the Russian Academy of Sciences, and NIH Fogarty grant 5 RO3 TW007210.",

year = "2008",

month = jun,

doi = "10.1134/S0006297908060035",

language = "English",

volume = "73",

pages = "644--651",

journal = "Biochemistry (Moscow)",

issn = "0006-2979",

publisher = "Pleiades Publishing",

number = "6",

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TY - JOUR

T1 - Analysis of proteins interacting with TRIP8b adapter

AU - Popova, N. V.

AU - Plotnikov, A. N.

AU - Ziganshin, R. Kh

AU - Deyev, I. E.

AU - Petrenko, A. G.

N1 - Funding Information: This work was financially supported by the Russian Foundation for Basic Research (grant No. 06 04 49706a), Fundamental Sciences for Medicine and Molecular and Cellular Biology Programs of Presidium of the Russian Academy of Sciences, and NIH Fogarty grant 5 RO3 TW007210.

PY - 2008/6

Y1 - 2008/6

N2 - Calcium-independent receptor of latrotoxin (CIRL) is an orphan heptahelical receptor implicated in regulation of exocytosis. To characterize molecular mechanisms of CIRL functioning, we searched for its intracellular partners using the yeast two-hybrid SR system with the cytoplasmic C-terminal fragment of CIRL as bait. One of the interacting proteins was identified as TRIP8b, a putative cytosolic adapter protein with multiple tetratricopeptide repeats. To understand functional significance of CIRL-TRIP8b interaction, we further isolated TRIP8b-interacting proteins by affinity chromatography of brain extracts on immobilized recombinant TRIP8b. Sixteen proteins were identified by mass spectrometry in the purified preparations. Clathrin and subunits of AP2 complex appeared to be the major TRIP8b-interacting proteins. Our data suggest a role of TRIP8b in receptor-mediated endocytosis.

AB - Calcium-independent receptor of latrotoxin (CIRL) is an orphan heptahelical receptor implicated in regulation of exocytosis. To characterize molecular mechanisms of CIRL functioning, we searched for its intracellular partners using the yeast two-hybrid SR system with the cytoplasmic C-terminal fragment of CIRL as bait. One of the interacting proteins was identified as TRIP8b, a putative cytosolic adapter protein with multiple tetratricopeptide repeats. To understand functional significance of CIRL-TRIP8b interaction, we further isolated TRIP8b-interacting proteins by affinity chromatography of brain extracts on immobilized recombinant TRIP8b. Sixteen proteins were identified by mass spectrometry in the purified preparations. Clathrin and subunits of AP2 complex appeared to be the major TRIP8b-interacting proteins. Our data suggest a role of TRIP8b in receptor-mediated endocytosis.

KW - CIRL/latrophilin

KW - Clathrin

KW - Endocytosis

KW - TRIP8b

UR - http://www.scopus.com/inward/record.url?scp=46449119261&partnerID=8YFLogxK

U2 - 10.1134/S0006297908060035

DO - 10.1134/S0006297908060035

M3 - Article

C2 - 18620529

AN - SCOPUS:46449119261

SN - 0006-2979

VL - 73

SP - 644

EP - 651

JO - Biochemistry (Moscow)

JF - Biochemistry (Moscow)

IS - 6

ER -

Analysis of proteins interacting with TRIP8b adapter

Abstract

Keywords

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