Universität zu Köln

Zhang, Jin-Li, Richetti, Stefania, Ramezani, Thomas, Welcker, Daniela, Luetke, Steffen, Pogoda, Hans-Martin, Hatzold, Julia, Zaucke, Frank, Keene, Douglas R., Bloch, Wilhelm, Sengle, Gerhard and Hammerschmidt, Matthias (2022). Vertebrate extracellular matrix protein hemicentin-1 interacts physically and genetically with basement membrane protein nidogen-2. Matrix Biol., 112. AMSTERDAM: ELSEVIER. ISSN 1569-1802

Full text not available from this repository.

Abstract

Hemicentins are large proteins of the extracellular matrix that belong to the fibulin family and play pivotal roles during development and homeostasis of a variety of invertebrate and vertebrate tissues. However, bona fide interaction partners of hemicentins have not been described as yet. Here, applying surface plasmon resonance spectroscopy and co-immunoprecipitation, we identify the basement membrane protein nidogen-2 (NID2) as a binding partner of mouse and zebrafish hemicentin-1 (HMCN1), in line with the formerly described essential role of mouse HMCN1 in basement membrane integrity. We show that HMCN1 binds to the same protein domain of NID2 (G2) as formerly shown for laminins, but with an approximately 3.5-fold lower affinity and in a competitive manner. Furthermore, immunofluorescence and immunogold labeling revealed that HMCN1/Hmcn1 is localized close to basement membranes and in partial overlap with NID2/Nid2a in different tissues of mouse and zebrafish. Genetic knockout and antisense-mediated knockdown studies in zebrafish further show that loss of Nid2a leads to similar defects in fin fold morphogenesis as the loss of Laminin-a5 (Lama5) or Hmcn1. Finally, combined partial loss-of-function studies indicated that nid2a genetically interacts with both hmcn1 and lama5. Together, these findings suggest that despite their mutually exclusive physical binding, hemicentins, nidogens, and laminins tightly cooperate and support each other during formation, maintenance, and function of basement membranes to confer tissue linkage. (C) 2022 Elsevier B.V. All rights reserved.

Item Type:	Journal Article
Creators:	Creators Email ORCID ORCID Put Code Zhang, Jin-Li UNSPECIFIED UNSPECIFIED UNSPECIFIED Richetti, Stefania UNSPECIFIED UNSPECIFIED UNSPECIFIED Ramezani, Thomas UNSPECIFIED UNSPECIFIED UNSPECIFIED Welcker, Daniela UNSPECIFIED UNSPECIFIED UNSPECIFIED Luetke, Steffen UNSPECIFIED UNSPECIFIED UNSPECIFIED Pogoda, Hans-Martin UNSPECIFIED UNSPECIFIED UNSPECIFIED Hatzold, Julia UNSPECIFIED UNSPECIFIED UNSPECIFIED Zaucke, Frank UNSPECIFIED UNSPECIFIED UNSPECIFIED Keene, Douglas R. UNSPECIFIED UNSPECIFIED UNSPECIFIED Bloch, Wilhelm UNSPECIFIED UNSPECIFIED UNSPECIFIED Sengle, Gerhard UNSPECIFIED UNSPECIFIED UNSPECIFIED Hammerschmidt, Matthias UNSPECIFIED UNSPECIFIED UNSPECIFIED
URN:	urn:nbn:de:hbz:38-679231
DOI:	10.1016/j.matbio.2022.08.009
Journal or Publication Title:	Matrix Biol.
Volume:	112
Date:	2022
Publisher:	ELSEVIER
Place of Publication:	AMSTERDAM
ISSN:	1569-1802
Language:	English
Faculty:	Unspecified
Divisions:	Unspecified
Subjects:	no entry
Uncontrolled Keywords:	Keywords Language CELL-MIGRATION; MOUSE NIDOGEN-2; FRASER-SYNDROME; BINDING; COLLAGEN; LAMININ; FIBULINS; DOMAINS; FAMILY; ROLES Multiple languages Biochemistry & Molecular Biology; Cell Biology Multiple languages
URI:	http://kups.ub.uni-koeln.de/id/eprint/67923