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  1. Article ; Online: Dissection of structural and functional requirements that underlie the interaction of ERdj3 protein with substrates in the endoplasmic reticulum.

    Otero, Joel H / Lizák, Beata / Feige, Matthias J / Hendershot, Linda M

    The Journal of biological chemistry

    2014  Volume 289, Issue 40, Page(s) 27504–27512

    Abstract: ERdj3, a mammalian endoplasmic reticulum (ER) Hsp40/DnaJ family member, binds unfolded proteins, transfers them to BiP, and concomitantly stimulates BiP ATPase activity. However, the requirements for ERdj3 binding to and release from substrates in cells ... ...

    Abstract ERdj3, a mammalian endoplasmic reticulum (ER) Hsp40/DnaJ family member, binds unfolded proteins, transfers them to BiP, and concomitantly stimulates BiP ATPase activity. However, the requirements for ERdj3 binding to and release from substrates in cells are not well understood. We found that ERdj3 homodimers that cannot stimulate the ATPase activity of BiP (QPD mutants) bound to unfolded ER proteins under steady state conditions in much greater amounts than wild-type ERdj3. This was due to reduced release from these substrates as opposed to enhanced binding, although in both cases dimerization was strictly required for substrate binding. Conversely, heterodimers consisting of one wild-type and one mutant ERdj3 subunit bound substrates at levels comparable with wild-type ERdj3 homodimers, demonstrating that release requires only one protomer to be functional in stimulating BiP ATPase activity. Co-expressing wild-type ERdj3 and a QPD mutant, which each exclusively formed homodimers, revealed that the release rate of wild-type ERdj3 varied according to the relative half-lives of substrates, suggesting that ERdj3 release is an important step in degradation of unfolded client proteins in the ER. Furthermore, pulse-chase experiments revealed that the binding of QPD mutant homodimers remained constant as opposed to increasing, suggesting that ERdj3 does not normally undergo reiterative binding cycles with substrates.
    MeSH term(s) Adenosine Triphosphatases/metabolism ; Animals ; COS Cells ; Chlorocebus aethiops ; Dimerization ; Endoplasmic Reticulum/chemistry ; Endoplasmic Reticulum/enzymology ; Endoplasmic Reticulum/genetics ; Endoplasmic Reticulum/metabolism ; HSP40 Heat-Shock Proteins/chemistry ; HSP40 Heat-Shock Proteins/genetics ; HSP40 Heat-Shock Proteins/metabolism ; Humans ; Kinetics ; Protein Binding ; Protein Folding ; Proteins/metabolism
    Chemical Substances DNAJB11 protein, human ; HSP40 Heat-Shock Proteins ; Proteins ; Adenosine Triphosphatases (EC 3.6.1.-)
    Language English
    Publishing date 2014-08-20
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1074/jbc.M114.587147
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Large 1p36 Deletions Affecting Arid1a Locus Facilitate Mycn-Driven Oncogenesis in Neuroblastoma.

    García-López, Jesus / Wallace, Kirby / Otero, Joel H / Olsen, Rachelle / Wang, Yong-Dong / Finkelstein, David / Gudenas, Brian L / Rehg, Jerold E / Northcott, Paul / Davidoff, Andrew M / Freeman, Kevin W

    Cell reports

    2019  Volume 30, Issue 2, Page(s) 454–464.e5

    Abstract: Loss of heterozygosity (LOH) at 1p36 occurs in multiple cancers, including neuroblastoma (NBL). MYCN amplification and 1p36 deletions tightly correlate with markers of tumor aggressiveness in NBL. Although distal 1p36 losses associate with single-copy ... ...

    Abstract Loss of heterozygosity (LOH) at 1p36 occurs in multiple cancers, including neuroblastoma (NBL). MYCN amplification and 1p36 deletions tightly correlate with markers of tumor aggressiveness in NBL. Although distal 1p36 losses associate with single-copy MYCN tumors, larger deletions correlate with MYCN amplification, indicating two tumor suppressor regions in 1p36, only one of which facilitates MYCN oncogenesis. To better define this region, we genome-edited the syntenic 1p36 locus in primary mouse neural crest cells (NCCs), a putative NBL cell of origin. In in vitro cell transformation assays, we show that Chd5 loss confers most of the MYCN-independent tumor suppressor effects of 1p36 LOH. In contrast, MYCN-driven tumorigenesis selects for NCCs with Arid1a deletions from a pool of NCCs with randomly sized 1p36 deletions, establishing Arid1a as the MYCN-associated tumor suppressor. Our findings reveal that Arid1a loss collaborates with oncogenic MYCN and better define the tumor suppressor functions of 1p36 LOH in NBL.
    MeSH term(s) Animals ; Chromosome Deletion ; Chromosome Disorders/genetics ; Chromosomes, Human, Pair 1/genetics ; DNA-Binding Proteins/metabolism ; Humans ; Mice ; N-Myc Proto-Oncogene Protein/metabolism ; Neuroblastoma/genetics ; Transcription Factors/metabolism
    Chemical Substances Arid1a protein, mouse ; DNA-Binding Proteins ; MYCN protein, human ; N-Myc Proto-Oncogene Protein ; Transcription Factors
    Language English
    Publishing date 2019-12-09
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 2649101-1
    ISSN 2211-1247 ; 2211-1247
    ISSN (online) 2211-1247
    ISSN 2211-1247
    DOI 10.1016/j.celrep.2019.12.048
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Life and death of a BiP substrate.

    Otero, Joel H / Lizák, Beáta / Hendershot, Linda M

    Seminars in cell & developmental biology

    2009  Volume 21, Issue 5, Page(s) 472–478

    Abstract: BiP is the mammalian endoplasmic reticulum (ER) Hsp70 orthologue that plays a major role in all functions of this organelle including the seemingly opposing functions of aiding the maturation of unfolded nascent proteins and identifying and targeting ... ...

    Abstract BiP is the mammalian endoplasmic reticulum (ER) Hsp70 orthologue that plays a major role in all functions of this organelle including the seemingly opposing functions of aiding the maturation of unfolded nascent proteins and identifying and targeting chronically unfolded proteins for degradation. The recent identification of mammalian BiP co-factors combined with delineation of the ER degradation machinery and data suggesting that the ER is subdivided into unique regions helps explain how these different functions can occur in the same organelle and raises some unresolved issues.
    MeSH term(s) Animals ; Endoplasmic Reticulum/metabolism ; HSP70 Heat-Shock Proteins/metabolism ; Humans
    Chemical Substances HSP70 Heat-Shock Proteins
    Language English
    Publishing date 2009-12-21
    Publishing country England
    Document type Journal Article ; Review
    ZDB-ID 1312473-0
    ISSN 1096-3634 ; 1084-9521
    ISSN (online) 1096-3634
    ISSN 1084-9521
    DOI 10.1016/j.semcdb.2009.12.008
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: ERdj4 protein is a soluble endoplasmic reticulum (ER) DnaJ family protein that interacts with ER-associated degradation machinery.

    Lai, Chunwei Walter / Otero, Joel H / Hendershot, Linda M / Snapp, Erik

    The Journal of biological chemistry

    2012  Volume 287, Issue 11, Page(s) 7969–7978

    Abstract: Protein localization within cells regulates accessibility for interactions with co-factors and substrates. The endoplasmic reticulum (ER) BiP co-factor ERdj4 is up-regulated by ER stress and has been implicated in ER-associated degradation (ERAD) of ... ...

    Abstract Protein localization within cells regulates accessibility for interactions with co-factors and substrates. The endoplasmic reticulum (ER) BiP co-factor ERdj4 is up-regulated by ER stress and has been implicated in ER-associated degradation (ERAD) of multiple unfolded secretory proteins. Several other ERdj family members tend to interact selectively with nascent proteins, presumably because those ERdj proteins associate with the Sec61 translocon that facilitates entry of nascent proteins into the ER. How ERdj4 selects and targets terminally misfolded proteins for destruction remains poorly understood. In this study, we determined properties of ERdj4 that might aid in this function. ERdj4 was reported to retain its signal sequence and to be resistant to mild detergent extraction, suggesting that it was an integral membrane protein. However, live cell photobleaching analyses of GFP-tagged ERdj4 revealed that the protein exhibits diffusion coefficients uncommonly high for an ER integral membrane protein and more similar to the mobility of a soluble luminal protein. Biochemical characterization established that the ERdj4 signal sequence is cleaved to yield a soluble protein. Importantly, we found that both endogenous and overexpressed ERdj4 associate with the integral membrane protein, Derlin-1. Our findings now directly link ERdj4 to the ERAD machinery and suggest a model in which ERjd4 could help recruit clients from throughout the ER to ERAD sites.
    MeSH term(s) Animals ; Cell Line ; Dogs ; Endoplasmic Reticulum/genetics ; Endoplasmic Reticulum/metabolism ; Endoplasmic Reticulum-Associated Degradation/physiology ; Intracellular Membranes/metabolism ; Membrane Glycoproteins/genetics ; Membrane Glycoproteins/metabolism ; Membrane Proteins/genetics ; Membrane Proteins/metabolism ; Mice ; Models, Biological ; Protein Sorting Signals/physiology ; Protein Transport/physiology
    Chemical Substances ERdj4 protein, mouse ; Membrane Glycoproteins ; Membrane Proteins ; Protein Sorting Signals ; derlin-1 protein, mouse
    Language English
    Publishing date 2012-01-20
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1074/jbc.M111.311290
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: Cancer Mutations of the Tumor Suppressor SPOP Disrupt the Formation of Active, Phase-Separated Compartments.

    Bouchard, Jill J / Otero, Joel H / Scott, Daniel C / Szulc, Elzbieta / Martin, Erik W / Sabri, Nafiseh / Granata, Daniele / Marzahn, Melissa R / Lindorff-Larsen, Kresten / Salvatella, Xavier / Schulman, Brenda A / Mittag, Tanja

    Molecular cell

    2018  Volume 72, Issue 1, Page(s) 19–36.e8

    Abstract: Mutations in the tumor suppressor SPOP (speckle-type POZ protein) cause prostate, breast, and other solid tumors. SPOP is a substrate adaptor of the cullin3-RING ubiquitin ligase and localizes to nuclear speckles. Although cancer-associated mutations in ... ...

    Abstract Mutations in the tumor suppressor SPOP (speckle-type POZ protein) cause prostate, breast, and other solid tumors. SPOP is a substrate adaptor of the cullin3-RING ubiquitin ligase and localizes to nuclear speckles. Although cancer-associated mutations in SPOP interfere with substrate recruitment to the ligase, mechanisms underlying assembly of SPOP with its substrates in liquid nuclear bodies and effects of SPOP mutations on assembly are poorly understood. Here, we show that substrates trigger phase separation of SPOP in vitro and co-localization in membraneless organelles in cells. Enzymatic activity correlates with cellular co-localization and in vitro mesoscale assembly formation. Disease-associated SPOP mutations that lead to the accumulation of proto-oncogenic proteins interfere with phase separation and co-localization in membraneless organelles, suggesting that substrate-directed phase separation of this E3 ligase underlies the regulation of ubiquitin-dependent proteostasis.
    MeSH term(s) Cell Compartmentation/genetics ; Cell Line, Tumor ; Humans ; Mutation ; Neoplasms/genetics ; Neoplasms/pathology ; Nuclear Proteins/genetics ; Proteostasis/genetics ; Repressor Proteins/genetics ; Ubiquitin/genetics ; Ubiquitin-Protein Ligases/genetics ; Ubiquitination/genetics
    Chemical Substances Nuclear Proteins ; Repressor Proteins ; SPOP protein, human ; Ubiquitin ; CULL-RING ligase, human (EC 2.3.2.27) ; Ubiquitin-Protein Ligases (EC 2.3.2.27)
    Language English
    Publishing date 2018-09-20
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 1415236-8
    ISSN 1097-4164 ; 1097-2765
    ISSN (online) 1097-4164
    ISSN 1097-2765
    DOI 10.1016/j.molcel.2018.08.027
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article: Interaction networks and the use of floral resources by male orchid bees (Hymenoptera: Apidae: Euglossini) in a primary rain forests of the Chocó Region (Colombia).

    Ospina-Torres, Rodulfo / Montoya-Pfeiffer, Paula María / Parra-H, Alejandro / Solarte, Victor / Tupac Otero, Joel

    Revista de biologia tropical

    2015  Volume 63, Issue 3, Page(s) 647–658

    Abstract: Orchid bees are important keystone pollinators from the Neotropics. With the aim to study the relationships between orchid bees and their nectar and aromatic host species, we made systematic samplings of males across two conservation areas in the ... ...

    Abstract Orchid bees are important keystone pollinators from the Neotropics. With the aim to study the relationships between orchid bees and their nectar and aromatic host species, we made systematic samplings of males across two conservation areas in the biogeographic Choc6 Region of Colombia. We used chemical baits to collect 352 male bees during five months. The pollen attached to their bodies was extracted for palynological identification and to estimate interaction networks. The euglossine community consisted of at least 22 species including Eg. maculilabris, Eg. orellana, Eg. championi and Eg. ignita. The male bees were associated with 84 plants but depended on a small group of them (Peperomia spp. and Anthurium spp, as well as species of Solanaceae, Ericaceae and Malpighiaceae) which were widely distributed across the altitudinal gradient, and were available through the year. The resulting interaction networks revealed a typical nested pattern usually found in plant-pollinator interactions, with several rare bee and plant species interaction with a small group of generalist bees and plant species. Albeit, we found variation within networks related to species composition. Such variation may be a consequence of specific differences in plant flowering phenology.
    MeSH term(s) Animals ; Bees/classification ; Bees/physiology ; Colombia ; Ecosystem ; Male ; Orchidaceae/classification ; Pollination ; Population Density ; Rainforest
    Language English
    Publishing date 2015-09
    Publishing country Costa Rica
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2020929-0
    ISSN 2215-2075 ; 0034-7744
    ISSN (online) 2215-2075
    ISSN 0034-7744
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Article ; Online: Int6 and Moe1 interact with Cdc48 to regulate ERAD and proper chromosome segregation.

    Otero, Joel H / Suo, Jinfeng / Gordon, Colin / Chang, Eric C

    Cell cycle (Georgetown, Tex.)

    2010  Volume 9, Issue 1, Page(s) 147–161

    Abstract: Int6/eIF3e is implicated in tumorigenesis, but its molecular functions remain unclear. We have studied its fission yeast homolog Yin6, reporting that it regulates proteolysis by controlling the assembly/localization of proteasomes, and binds directly to ... ...

    Abstract Int6/eIF3e is implicated in tumorigenesis, but its molecular functions remain unclear. We have studied its fission yeast homolog Yin6, reporting that it regulates proteolysis by controlling the assembly/localization of proteasomes, and binds directly to another conserved protein, Moe1. In the present study, we isolated Cdc48 as a Moe1-binding protein from a yeast two-hybrid screen, and confirmed biochemically that they form a stable complex in fission yeast. Overexpressing Moe1 or Yin6 partially rescued phenotypes of cdc48 mutants; conversely, overexpressing Cdc48 partially rescued phenotypes of moe1 or yin6 mutants. Mutants defective in both Cdc48 and the Yin6-Moe1 complex showed growth defects that were far more severe than either alone. These double mutants were severely deficient in endoplasmic reticulum associated degradation (ERAD), as they were hypersensitive to accumulation of misfolded proteins. In addition, their chromosomes showed frequent defects in spindle attachment and segregation--these mitotic defects correlated with Ase1 and Bir1/survivin mislocalization. These results suggest that Cdc48, Yin6 and Moe1 act in the same protein complex to concertedly control ERAD and chromosome segregation. Many of these properties are evolutionarily conserved in humans, since human Cdc48 rescued the lethality of the yeast cdc48Delta mutant, and Int6 and Moe1/eIF3d bind Cdc48 in human cells.
    MeSH term(s) Adenosine Triphosphatases/genetics ; Adenosine Triphosphatases/metabolism ; Blotting, Far-Western ; Carrier Proteins/genetics ; Carrier Proteins/metabolism ; Cell Cycle Proteins/genetics ; Cell Cycle Proteins/metabolism ; Chromosome Segregation/genetics ; Chromosome Segregation/physiology ; Eukaryotic Initiation Factors/genetics ; Eukaryotic Initiation Factors/metabolism ; Humans ; Immunoprecipitation ; Protein Binding/physiology ; Schizosaccharomyces pombe Proteins/genetics ; Schizosaccharomyces pombe Proteins/metabolism ; Two-Hybrid System Techniques ; Valosin Containing Protein
    Chemical Substances Carrier Proteins ; Cell Cycle Proteins ; Eukaryotic Initiation Factors ; Moe1 protein, S pombe ; Schizosaccharomyces pombe Proteins ; int6 protein, S pombe ; Adenosine Triphosphatases (EC 3.6.1.-) ; Valosin Containing Protein (EC 3.6.4.6)
    Language English
    Publishing date 2010-01-09
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 2146183-1
    ISSN 1551-4005 ; 1538-4101 ; 1554-8627
    ISSN (online) 1551-4005
    ISSN 1538-4101 ; 1554-8627
    DOI 10.4161/cc.9.1.10312
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Article ; Online: Interaction networks and the use of floral resources by male orchid bees (Hymenoptera

    Rodulfo Ospina-Torres / Paula María Montoya-Pfeiffer / Alejandro Parra-H. / Víctor Solarte / Joel Tupac Otero

    Revista de Biología Tropical, Vol 63, Iss 3, Pp 647-

    Apidae: Euglossini) in a primary rain forests of the Chocó Region (Colombia)

    2015  Volume 658

    Abstract: Orchid bees are important keystone pollinators from the Neotropics. With the aim to study the relationships between orchid bees and their nectar and aromatic host species, we made systematic samplings of males across two conservation areas in the ... ...

    Abstract Orchid bees are important keystone pollinators from the Neotropics. With the aim to study the relationships between orchid bees and their nectar and aromatic host species, we made systematic samplings of males across two conservation areas in the biogeographic Chocó Region of Colombia. We used chemical baits to collect 352 male bees during five months. The pollen attached to their bodies was extracted for palynological identification and to estimate interaction networks. The euglossine community consisted of at least 22 species including Eg. maculilabris, Eg. orellana, Eg. championiand Eg. ignita.The male bees were associated with 84 plants but depended on a small group of them (Peperomiaspp. and Anthuriumspp, as well as species of Solanaceae, Ericaceae and Malpighiaceae) which were widely distributed across the altitudinal gradient, and were available through the year. The resulting interaction networks revealed a typical nested pattern usually found in plant-pollinator interactions, with several rare bee and plant species interaction with a small group of generalist bees and plant species. Albeit, we found variation within networks related to species composition. Such variation may be a consequence of specific differences in plant flowering phenology.
    Keywords polinizadores ; redes de interacciones ; relación planta-insecto ; Reserva Natural del Río Ñambí ; Biology (General) ; QH301-705.5
    Subject code 590 ; 580
    Language English
    Publishing date 2015-09-01T00:00:00Z
    Publisher Vicerractoría Investigación
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  9. Article: Cancer Mutations of the Tumor Suppressor SPOP Disrupt the Formation of Active, Phase-Separated Compartments

    Bouchard, Jill J / Otero, Joel H / Scott, Daniel C / Szulc, Elzbieta / Martin, Erik W / Sabri, Nafiseh / Granata, Daniele / Marzahn, Melissa R / Lindorff-Larsen, Kresten / Salvatella, Xavier / Schulman, Brenda A / Mittag, Tanja

    Molecular cell. 2018 Oct. 04, v. 72, no. 1

    2018  

    Abstract: Mutations in the tumor suppressor SPOP (speckle-type POZ protein) cause prostate, breast, and other solid tumors. SPOP is a substrate adaptor of the cullin3-RING ubiquitin ligase and localizes to nuclear speckles. Although cancer-associated mutations in ... ...

    Abstract Mutations in the tumor suppressor SPOP (speckle-type POZ protein) cause prostate, breast, and other solid tumors. SPOP is a substrate adaptor of the cullin3-RING ubiquitin ligase and localizes to nuclear speckles. Although cancer-associated mutations in SPOP interfere with substrate recruitment to the ligase, mechanisms underlying assembly of SPOP with its substrates in liquid nuclear bodies and effects of SPOP mutations on assembly are poorly understood. Here, we show that substrates trigger phase separation of SPOP in vitro and co-localization in membraneless organelles in cells. Enzymatic activity correlates with cellular co-localization and in vitro mesoscale assembly formation. Disease-associated SPOP mutations that lead to the accumulation of proto-oncogenic proteins interfere with phase separation and co-localization in membraneless organelles, suggesting that substrate-directed phase separation of this E3 ligase underlies the regulation of ubiquitin-dependent proteostasis.
    Keywords breasts ; enzyme activity ; liquids ; mutation ; neoplasms ; organelles ; proteins ; separation ; ubiquitin-protein ligase
    Language English
    Dates of publication 2018-1004
    Size p. 19-36.e8.
    Publishing place Elsevier Inc.
    Document type Article
    ZDB-ID 1415236-8
    ISSN 1097-4164 ; 1097-2765
    ISSN (online) 1097-4164
    ISSN 1097-2765
    DOI 10.1016/j.molcel.2018.08.027
    Database NAL-Catalogue (AGRICOLA)

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  10. Article: A tropical epiphytic orchid uses a low‐light interception strategy in a spatially heterogeneous light environment

    Ventre‐Lespiaucq, Agustina B / Adrián Escudero / Joel T. Otero / Juan A. Delgado / Luis Balaguer / María A. Sánchez / Nhora H. Ospina‐Calderón / Nicola S. Flanagan

    Biotropica. 2017 May, v. 49, no. 3

    2017  

    Abstract: Light is considered a non‐limiting factor for vascular epiphytes. Nevertheless, an epiphyte's access to light may be limited by phorophyte shading and the spatio‐temporal environmental patchiness characteristic of epiphytic habitats. We assessed the ... ...

    Abstract Light is considered a non‐limiting factor for vascular epiphytes. Nevertheless, an epiphyte's access to light may be limited by phorophyte shading and the spatio‐temporal environmental patchiness characteristic of epiphytic habitats. We assessed the extent to which potential light interception in Rodriguezia granadensis, an epiphytic orchid, is determined by individual factors (plant size traits and leaf traits), or environmental heterogeneity (light patchiness) within the crown of the phorophyte, or both. We studied 104 adult plants growing on Psidium guajava trees in two habitats with contrasting canopy cover: a dry tropical forest edge, and isolated trees in a pasture. We recorded the number of leaves and the leaf area, the leaf position angles, and the potential exposure of the leaf surface to direct irradiance (silhouette area of the leaf blade), and the potential irradiance incident on each plant. We found the epiphytes experience a highly heterogeneous light environment in the crowns of P. guajava. Nonetheless, R. granadensis plants displayed a common light interception strategy typical of low‐light environments, resembling terrestrial, forest understory plants. Potential exposure of the total leaf surface to direct irradiance correlated positively with plant size and within‐plant variation in leaf orientation. In many‐leaved individuals, within‐plant variation in leaf angles produced complementary leaf positions that enhanced potential light interception. This light interception strategy suggests that, in contrast to current wisdom, enhancing light capture is important for vascular epiphytes in canopies with high spatio‐temporal heterogeneity in light environments.
    Keywords canopy ; edge effects ; epiphytes ; habitats ; leaf angle ; leaf area ; leaf blade ; light intensity ; mature plants ; Orchidaceae ; pastures ; Psidium guajava ; shade ; trees ; tropical forests ; understory
    Language English
    Dates of publication 2017-05
    Size p. 318-327.
    Publishing place John Wiley & Sons, Ltd
    Document type Article
    Note JOURNAL ARTICLE
    ZDB-ID 2052061-X
    ISSN 1744-7429 ; 0006-3606
    ISSN (online) 1744-7429
    ISSN 0006-3606
    DOI 10.1111/btp.12425
    Database NAL-Catalogue (AGRICOLA)

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