Universität zu Köln

Begonja, Antonija Jurak ORCID: 0000-0001-5798-0888, Pluthero, Fred G., Suphamungmee, Worawit, Giannini, Silvia, Christensen, Hilary, Leung, Richard, Lo, Richard W., Nakamura, Fumihiko ORCID: 0000-0002-6872-4246, Lehman, William, Plomann, Markus, Hoffmeister, Karin M., Kahr, Walter H. A., Hartwig, John H. and Falet, Herve ORCID: 0000-0003-0788-9204 (2015). FlnA binding to PACSIN2 F-BAR domain regulates membrane tubulation in megakaryocytes and platelets. Blood, 126 (1). S. 80 - 89. WASHINGTON: AMER SOC HEMATOLOGY. ISSN 1528-0020

Full text not available from this repository.

Abstract

Bin-Amphiphysin-Rvs (BAR) and Fes-CIP4 homology BAR (F-BAR) proteins generate tubular membrane invaginations reminiscent of the megakaryocyte (MK) demarcation membrane system (DMS), which provides membranes necessary for future platelets. The F-BAR protein PACSIN2 is one of the most abundant BAR/F-BAR proteins in platelets and the only one reported to interact with the cytoskeletal and scaffold protein filamin A (FlnA), an essential regulator of platelet formation and function. The FlnA-PACSIN2 interaction was therefore investigated in MKs and platelets. PACSIN2 associated with FlnA in human platelets. The interaction required FlnA immunoglobulin-like repeat 20 and the tip of PACSIN2 F-BAR domain and enhanced PACSIN2 F-BAR domain membrane tubulation in vitro. Most human and wild-type mouse platelets had 1 to 2 distinct PACSIN2 foci associated with cell membrane GPIb alpha, whereas Flna-null platelets had 0 to 4 or more foci. Endogenous PACSIN2 and transfected enhanced green fluorescent protein-PACSIN2 were concentrated in midstage wild-type mouse MKs in a well-defined invagination of the plasma membrane reminiscent of the initiating DMS and dispersed in the absence of FlnA binding. The DMS appeared less well defined, and platelet territories were not readily visualized in Flna-null MKs. We conclude that the FlnA-PACSIN2 interaction regulates membrane tubulation in MKs and platelets and likely contributes to DMS formation.

Item Type:	Journal Article
Creators:	Creators Email ORCID ORCID Put Code Begonja, Antonija Jurak UNSPECIFIED orcid.org/0000-0001-5798-0888 UNSPECIFIED Pluthero, Fred G. UNSPECIFIED UNSPECIFIED UNSPECIFIED Suphamungmee, Worawit UNSPECIFIED UNSPECIFIED UNSPECIFIED Giannini, Silvia UNSPECIFIED UNSPECIFIED UNSPECIFIED Christensen, Hilary UNSPECIFIED UNSPECIFIED UNSPECIFIED Leung, Richard UNSPECIFIED UNSPECIFIED UNSPECIFIED Lo, Richard W. UNSPECIFIED UNSPECIFIED UNSPECIFIED Nakamura, Fumihiko UNSPECIFIED orcid.org/0000-0002-6872-4246 UNSPECIFIED Lehman, William UNSPECIFIED UNSPECIFIED UNSPECIFIED Plomann, Markus UNSPECIFIED UNSPECIFIED UNSPECIFIED Hoffmeister, Karin M. UNSPECIFIED UNSPECIFIED UNSPECIFIED Kahr, Walter H. A. UNSPECIFIED UNSPECIFIED UNSPECIFIED Hartwig, John H. UNSPECIFIED UNSPECIFIED UNSPECIFIED Falet, Herve UNSPECIFIED orcid.org/0000-0003-0788-9204 UNSPECIFIED
URN:	urn:nbn:de:hbz:38-399031
DOI:	10.1182/blood-2014-07-587600
Journal or Publication Title:	Blood
Volume:	126
Number:	1
Page Range:	S. 80 - 89
Date:	2015
Publisher:	AMER SOC HEMATOLOGY
Place of Publication:	WASHINGTON
ISSN:	1528-0020
Language:	English
Faculty:	Unspecified
Divisions:	Unspecified
Subjects:	no entry
Uncontrolled Keywords:	Keywords Language RECEPTOR-MEDIATED ENDOCYTOSIS; ACTIN ORGANIZATION; STRUCTURAL BASIS; MOLECULAR-BASIS; SYNDAPIN-II; PROTEIN; FILAMIN; SYSTEM; INVAGINATION; CURVATURE Multiple languages Hematology Multiple languages
URI:	http://kups.ub.uni-koeln.de/id/eprint/39903